- Home - Introduction - Projects - People - Publications - Vacancies -

2009

The RecB nuclease domain binds to RecA-DNA filaments: implications for filament loading.
Lucarelli, D., Wang, Y.A., Galkin, V.E., Yu, X., Wigley, D.B., Egelman, E.H. (2009)
J. Mol. Biol. 391, 269-274.

Mechanistic basis of 5'-3' translocation in SF1B helicases.
Saikrishnan, K., Powell, B., Cook, N.J., Webb, M.R., Wigley, D.B. (2009)
Cell 137, 849-859.

ORC proteins: marking the start.
Wigley, D.B. (2009)
Curr. Op. Struct. Biol. 19, 72-78.

2008

The glutamate switch provides a link between ATPase activity and ligand binding in AAA+ proteins.
Zhang, X., Wigley, D.B. (2008)
Nat Struct Mol Biol. 15, 1223-1227.

DNA binding to RecD: role of the 1B domain in SF1B helicase activity.
Saikrishnan, K., Griffith, S.P., Cook, N., Court, R., Wigley, D.B. (2008)
EMBO J. 27, 2222-2229.

2007

RecBCD: The Supercar of DNA Repair.
Dale B. Wigley (2007)
Cell 131, 651-653.

Structural Basis of DNA Replication Origin Recognition by an ORC Protein.
Gaudier, M., Schuwirth, B.S., Westcott, S.L. and Wigley, D.B. (2007)
Science 317, 1213-1216. [Abstract] [Full Text]

The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition.
Court, R., Cook, N., Saikrishnan, K. and Wigley, D.B. (2007)
J. Mol. Biol. 371, 25-33.

Structure and Mechanism of Helicases and Nucleic Acid Translocases.
Singleton, M.R., Dillingham, M.S., Wigley, D.B. (2007)
Annu Rev Biochem. 76, 23-50.

2006

Communication between subunits within an archaeal clamp-loader complex.
Seybert, A., Singleton, M.R., Cook, N., Hall, D.R. and Wigley, D.B. (2006).
EMBO J. 25, 2209-2218.

Biochemical analysis of a DNA replication origin in the Archaeon Aeropyrum pernix.
Grainge, I., Gaudier, M., Schuwirth, B.S., Westcott, S.L., Sandall, J., Atanassova, N. and Wigley, D.B. (2006)
J. Mol. Biol. 363, 355-369.

CeBRC-2 stimulates D-loop formation by RAD-51 and promotes DNA single-strand annealing.
Petalcorin, M.I., Sandall, J., Wigley, D.B. and Boulton, S.J. (2006)
J. Mol. Biol. 361, 231-242.

2005

Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase.
Takahashi, T.S., Wigley, D.B. and Walter, J.C. (2005).
Trends Bioch. Sci. 30, 437-444.

2004

Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks.
Singleton, M.R., Dillingham, M.S., Gaudier, M., Kowalczykowski, S.C. and Wigley, D.B. (2004).
Nature 432, 187-193.

Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader.
Seybert, A. and Wigley, D.B. (2004)
EMBO J. 23, 1360-1371.

Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix.
Singleton, M.R., Morales, R., Grainge, I., Cook, N., Isupov, M.N. and Wigley, D.B. (2004)
J. Mol. Biol. 343, 547-557.

2003

Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes.
Singleton, M.R. and Wigley, D.B. (2003)
EMBO J. 22, 4579-4583.

Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus.
Grainge, I., Scaife, S. and Wigley, D.B. (2003)
Nucl. Acids Res. 31, 4888-4898.

2002

Structure of the single-strand annealing domain of human RAD52 protein.
Singleton, M.R., Wentzell, L.M., Liu, Y., West, S.C. and Wigley, D.B. (2002)
Proc. Natl. Acad. Sci.(USA) 99, 13492-13497.

Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeote Archaeoglobus fulgidus.
Seybert, A., Scott, D.J., Scaife, S., Singleton, M.R. and Wigley, D.B. (2002).
Nucl. Acids Res. 30, 4329-4338.

Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.
Soultanas, P. and Wigley, D.B. (2002).
Nucl. Acids Res. 30, 4051-4060.

The beta propeller protein YxaL increases the processivity of PcrA helicase.
Noirot-Gros, M., Soultanas, P., Wigley, D.B., Ehrlich, S.D., Noirot, P. and Petit, M. (2002).
Mol. Genet. Genom. 267, 391-400.

Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.
Polard, P., Marsin, S., McGovern, S., Velten, M., Wigley, D.B., Ehrlich, S.D. and Bruand, C. (2002).
Nucl. Acids Res. 30, 1593-1606.

Direct measurement of single-stranded DNA Translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine.
Dillingham, M.S., Wigley, D.B. and Webb, M.R. (2002).
Biochemistry 41, 643-651.

Modularity and specialization in Superfamily 1 and 2 helicases
Singleton, M.R. and Wigley, D.B. (2002).
J. Bacteriol. 184, 1819-1826.

2001

Structural analysis of DNA replication fork reversal by RecG.
Singleton, M.R., Scaife, S. and Wigley, D.B. (2001).
Cell 107, 79-89.

Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase.
Dillingham, M.S., Soultanas, P., Wiley, P., Webb, M.R. and Wigley, D.B. (2001).
Proc. Natl. Acad. Sci. (USA) 98, 8381-8387.

RadA Protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination.
McIlwraith, M.J., Hall, D.R., Stasiak, A.Z., Stasiak, A., Wigley, D.B. and West, S.C. (2001).
Nucl. Acids Res. 29, 4509-4517.

Crystallization and preliminary X-ray analysis of RecG, a replication-fork reversal helicase from Thermotoga maritima complexed with a three-way DNA junction.
Singleton, M.R., Scaife, S., Raven, N.D. and Wigley, D.B. (2001).
Acta Cryst. D57, 1695-1696.

Unwinding the "Gordian knot" of helicase action.
Soultanas, P. and Wigley, D.B. (2001).
Trends Bioch. Sci. 26, 47-54.

2000

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides.
Singleton, M.R., Sawaya, M.R., Ellenberger, T. and Wigley, D.B. (2000).
Cell 101, 589-600.

Uncoupling DNA translocation and helicase activity in PcrA : direct evidence for an active mechanism.
Soultanas, P., Dillingham, M.S., Wiley, P., Webb, M.R. and Wigley, D.B. (2000).
EMBO J. 19, 3799-3810.

Demonstration of unidirectional single stranded DNA translocation by PcrA helicase : measurement of step size and translocation speed.
Dillingham, M.S., Wigley, D.B. and Webb, M.R. (2000).
Biochemistry 39, 205-212.

Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase.
Pan, H. and Wigley, D.B. (2000).
Structure 8, 231-9.

DNA helicases : "inching forward".
Soultanas, P. and Wigley, D.B. (2000).
Curr. Op. Struct. Biol. 10, 124-128.

DNA ligases in the repair and replication of DNA.
Timson, D.J., Singleton, M.R. and Wigley, D.B. (2000).
Mutation Res. 460, 301-318.

DNA helicases : one small step for PcrA, one giant leap for RecBC ?
Wigley, D.B. (2000).
Current Biology 10, R444-R445.

High resolution refinement of [beta]-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for [alpha]-complementation.
Juers, D.H., Jacobson, R.H., Wigley, D.B., Zhang, X., Huber, R.E., Tronrud, D.E. and Matthews, B.W. (2000).
Protein Science 9, 1685-1699.

1999

Crystal structures of complexes of PcrA helicase with a DNA substrate indicate an inchworm mechanism.
Velankar, S.S., Soultanas, P., Dillingham, M.S., Subramanya, H.S. and Wigley, D.B. (1999).
Cell 97, 75-84.

Structure of the adenylation domain of an NAD-dependent DNA ligase.
Singleton, M.R., Håkansson, K., Timson, D.J. and Wigley, D.B. (1999).
Structure 7, 35-42.

Functional domains of an ATP-dependent DNA ligase.
Doherty, A.J. and Wigley, D.B. (1999).
J. Mol. Biol. 285, 63-71.

Functional domains of an NAD-dependent DNA ligase.
Timson, D.J. and Wigley, D.B. (1999).
J. Mol. Biol. 285, 73-81.

DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase.
Soultanas, P., Dillingham, M.S., Velankar, S.S. and Wigley, D.B. (1999).
J. Mol. Biol. 290, 137-148.

Plasmid replication initiator protein RepD increases the processivity of PcrA DNA helicase.
Soultanas, P., Dillingham, M.S., Papadopoulos, F., Phillips, S.E.V., Thomas, C.D. and Wigley, D.B. (1999).
Nucl. Acids Res. 27, 1421-1428.

Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation.
Dillingham, M.S., Soultanas, P. and Wigley, D.B. (1999).
Nucl. Acids Res. 27, 3310-3317.

The Bacillus stearothermophilus replicative helicase : cloning, overexpression and activity.
Bird, L.E. and Wigley, D.B. (1999).
Biochim. Biophys. Acta 1444, 424-428.

Cloning, expression and purification of Bacillus stearothermophilus DNA primase and crystallisation of the zinc-binding domain.
Pan, H., Bird, L.E. and Wigley, D.B. (1999).
Biochim. Biophys. Acta 1444, 429-433.

Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus.
Brannigan, J.A., Ashford, S.R., Doherty, A.J., Timson, D.J. and Wigley, D.B. (1999).
Biochim. Biophys. Acta 1432, 413-8.

1998

Conserved themes but novel activities in recombinases and topoisomerases.
Sherratt, D.J. and Wigley, D.B. (1998).
Cell 93, 149-152.

Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping.
Håkansson, K. and Wigley, D. B. (1998).
Proc. Natl. Acad. Sci. (USA) 95, 1505-1510.

The E.coli ribosomal protein L3 stimulates the helicase activity of the B.stearothermophilus PcrA helicase.
Soultanas, P., Dillingham, M.S. and Wigley, D.B. (1998).
Nucl. Acids Res. 26, 2374-2379.

Characterisation of Bacillus stearothermophilus PcrA helicase : evidence against an active rolling model.
Bird, L.E., Brannigan, J.A., Subramanya, H.S. and Wigley, D.B. (1998).
Nucl. Acids Res. 26, 2686-2693.

Teaching a new dog old tricks ?
Wigley, D.B. (1998).
Structure 6, 543-548.

Helicases : a unifying structural theme ?
Bird, L.E., Subramanya, H.S. and Wigley, D.B. (1998).
Curr. Op. Struct. Biol. 8, 14-18.

1997

X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzyme.
Håkansson, K., Doherty, A.J., Shuman, S. and Wigley, D.B. (1997).
Cell 89, 545-553.

Crystal structure of the site-specific recombinase, XerD.
Subramanya, H.S., Arciszewska, L.K., Baker, R.A., Bird, L.E., Sherratt, D.J.
and Wigley, D.B. (1997).
EMBO J. 16, 5178-5187.

The high resolution crystal structure of a 24 kDa gyrase B fragment from E.coli complexed with one of the most potent coumarin inhibitors, clorobiocin.
Tsai, F.T.F, Singh, O.M.P., Skarzynski, T., Wonacott, A.J., Weston, S., Tucker, A., Pauptit, R.A., Breeze, A.L., Poyser, J.P., O'Brien, R., Ladbury, J.E. and Wigley, D.B. (1997).
Proteins 28, 41-52.

Characterisation and crystallisation of the helicase domain of T7 gene 4 protein.
Bird, L.E., Håkansson, K., Pan, H. and Wigley, D.B. (1997).
Nucl. Acids Res. 25, 2020-2026.

Crystallisation of the RNA guanyltransferase of Chlorella virus PBCV-1.
Doherty, A.J., Håkansson, K., Ho, C.K., Shuman, S. and Wigley, D.B. (1997).
Acta Cryst. D53, 482-484.

1996

Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7.
Subramanya, H.S., Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996).
Cell 85, 607-615.

Crystal structure of a DExx box DNA helicase.
Subramanya, H.S., Bird, L.E., Brannigan, J.A. and Wigley, D.B. (1996).
Nature 384, 379-383.

The nature of inhibition of DNA gyrase by the coumarins and cyclothialidines revealed by X-ray crystallography.
Lewis, R.J., Singh, O.M.P., Smith, C.V., Skarzynski, T., Maxwell, A., Wonacott, A.J. and Wigley, D.B. (1996).
EMBO J. 15, 1412-1420.

Enzymatic ketonisation of 2-hydroxymuconate : mechanism and specificity investigated by the crystal structures of two isomerases.
Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S.
and Wigley, D.B. (1996).
Biochemistry 35, 792-802.

Bacteriophage T7 DNA ligase: overexpression, purification, crystallization and characterization.
Doherty, A.J., Ashford, S.R., Subramanya, H.S. and Wigley, D.B. (1996).
J. Biol. Chem. 271, 11083-11089.

Characterisation of proteolytic fragments of bacteriophage T7 DNA ligase.
Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996).
Nucl. Acids Res. 24, 2281-2287.

Mechanism of drug inhibition of DNA gyrase.
Lewis, R.J., Tsai, F.T.F. and Wigley, D.B. (1996).
Bioessays 18, 661-671.

A wasp head with a relaxing bite.
Wigley, D.B. (1996).
Structure 4, 117-120.

Crystallisation and preliminary crystallographic analysis of the DNA gyrase B protein from B.stearothermophilus.
Tsai, F.T.F., Subramanya, H.S., Brannigan, J.A., Wilkinson, A.J. and Wigley, D.B. (1996).
Acta Cryst. D52, 1216-1218.

Preliminary crystallographic analysis of the ParE subunit of E.coli topoisomerase IV.
Subramanya, H.S., Peng, H., Marians, K.J. and Wigley, D.B. (1996).
Acta Cryst. D52, 579-580.

1995

Structure and mechanism of DNA topoisomerases.
Wigley, D.B. (1995).
Ann. Rev. Biophys. Biomolec. Struct. 24, 185-208.

Structure and mechanism of DNA gyrase.
Wigley, D.B. (1995).
In "Nucleic Acids & Molecular Biology", Ed. F. Eckstein & D.M.J. Lilley, Springer-Verlag, pp 165-176.

A superior host strain for the overexpression of cloned genes using the T7 promoter based vectors.
Doherty, A.J., Ashford, S.R., Brannigan, J.A. and Wigley, D.B. (1995).
Nucl. Acids Res. 23, 2074-2075.

1994

Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by X-ray crystallographic analysis of a mutant designed to prevent tetramerisation.
Cameron, A.D., Roper, D.I., Moreton, K.M., Muirhead, H., Holbrook, J.J. and Wigley, D.B. (1994).
J. Mol. Biol. 238, 615-625.

The third IgG-binding domain from Streptococcal protein G : an analysis by X-ray crystallography of the structure alone and in a complex with Fab.
Derrick, J.P. and Wigley, D.B. (1994).
J. Mol. Biol. 243, 906-918.

Three-dimensional model of the gyrase B subunit crystallised in two-dimensions on novobiocin-linked phospholipid films.
Celia, H., Hoermann, L., Lebeau, L., Mallouh, V., Wigley, D.B., Wang, J.C., Mioskowski, C. and Oudet, P. (1994).
J. Mol. Biol. 236, 399-404.

Crystallisation of inhibitor complexes of an N-terminal 24kDa fragment of the DNA gyrase B protein.
Lewis, R.J., Singh, O.M.P., Smith, C.V., Maxwell, A., Skarzynski, T., Wonacott, A.J. and Wigley, D.B. (1994).
J. Mol. Biol. 241, 128-30.

Preliminary crystallographic analysis of 4-oxalocrotonate tautomerase reveals the oligomeric structure of the enzyme.
Roper, D.I., Subramanya, H.S., Shingler, V. and Wigley, D.B. (1994).
J. Mol. Biol. 243, 799-801.

1993

Analysis of bacterial immunoglobulin-binding proteins by X-ray crystallography.
Derrick, J.P. and Wigley, D.B. (1993).
Immunomethods 2, 9-16.

Structure and mechanism of Streptococcal protein G.
Derrick, J.P., Wigley, D.B., Lian, L-Y., Sutcliffe, M.J., Yang, J-C., Dawson, P.D. and Roberts, G.C.K. (1993).
Biochem. Soc. Trans. 21, 333.

1992

1991

Crystal structure of an N-terminal fragment of the DNA gyrase B protein.
Wigley, D.B., Davies, G.J., Dodson, E.J., Maxwell, A. and Dodson G.G. (1991).
Nature 351, 624-629.

Preliminary crystallographic analysis of the ATP-hydrolysing domain of the Escherichia coli DNA gyrase B protein.
Jackson, A.P., Maxwell, A. and Wigley, D.B. (1991).
J. Mol. Biol. 217, 15-17.

1990

Cloning of the DNA gyrase genes under tac promoter control : overproduction of the gyrase A and B proteins.
Hallett, P.A., Grimshaw, A.J., Wigley, D.B. and Maxwell, A. (1990).
Gene 93, 139-42.

The serine acetyltransferase from Escherichia coli : Overexpression, purification and preliminary crystallographic analysis.
Wigley, D.B., Derrick, J.P. and Shaw, W.V. (1990).
FEBS Letts. 277, 267-71.

Preliminary crystallographic analysis of the breakage-reunion domain of the Escherichia coli DNA gyrase A protein.
Reece, R.J., Dauter, Z., Wilson, K.S., Maxwell, A. and Wigley, D.B. (1990).
J. Mol. Biol. 215, 493-5.

Structure and function of the RepD protein of plasmid pC221.
Thomas, C.D., Balson, D.F., Wigley, D.B. and Shaw, W.V. (1990).
In "Molecular Biology of Staphylococci" Ed. Novick and Skurray. VCH Publishers, Inc., New York, pp 211-8.

1989

Preliminary crystallographic analysis of 5-carboxymethyl-2-hydroxymuconate isomerase from E.coli.
Wigley, D.B., Roper, D.I. and Cooper, R.A. (1989).
J. Mol. Biol. 210, 883-4.

Lactate Dehydrogenase. Effects of amino acid changes on properties.
Scawen, M.D., Barstow, D.A., Nichols, D.J., Atkinson, T., Clarke, A.R., Wigley, D.B., Hart, K., Chia, W.N. and Holbrook, J.J. (1989).
In "Advances in Protein Design". Ed. H. Bloecker, J. Collins, R.D. Schmid, and D. Schomburg, VCH Publishers, Weinheim. Monograph Vol. 12, pp 103-115.

1988

The use of genetically engineered tryptophan to identify the movement of a domain of B.stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme.
Waldman, A.D.B., Hart, K.W.,Clarke, A.R., Wigley, D.B., Barstow, D.A., Atkinson, T., Chia, W.N. and Holbrook, J.J. (1988).
Biochem. Biophys. Res. Comm. 150, 752-9.

Crystallisation of a ternary complex of lactate dehydrogenase from Bacillus stearothermophilus.
Wigley, D.B., Muirhead, H., Gamblin, S.J. and Holbrook, J.J. (1988).
J. Mol. Biol. 204, 1041-44.

1987

Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase.
Clarke, A.R., Wigley, D.B., Barstow, D.A., Chia, W.N., Waldman, A.D.B., Hart, K.W., Atkinson, T. and Holbrook, J.J. (1987).
Biochem. Soc. Trans. 15, 152-3.

A single amino acid substitution de-regulates a bacterial lactate dehydrogenase and stabilises its tetrameric structure.
Clarke, A.R., Wigley, D.B., Barstow, D.A., Chia, W.N., Atkinson, T. and Holbrook, J.J. (1987).
Biophys. Biochim. Acta 913, 72-80.

The use of site-directed mutagenesis and time resolved fluorescence spectroscopy to assign the fluorescence contributions of individual tryptophan residues in B.stearothermophilus lactate dehydrogenase.
Waldman, A.D.B., Clark, A.R., Wigley, D.B., Hart, K.W., Chia, W.N., Barstow, D.A., Atkinson, T., Munro, I. and Holbrook, J.J. (1987).
Biophys. Biochim. Acta 913, 66-71.

A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase.
Hart, K.W., Clarke, A.R., Wigley, D.B., Waldman, A.D.B., Chia, W.N., Barstow, D.A., Atkinson, T., Jones, J.B. and Holbrook, J.J. (1987).
Biophys. Biochim. Acta 914, 294-298.

The importance of arginine-171 in substrate binding in lactate dehydrogenase.
Hart, K.W., Clarke, A.R., Wigley, D.B., Chia, W.N., Barstow, D.A., Atkinson, T. and Holbrook, J.J. (1987).
Biochem. Biophys. Res. Comm. 146, 346-53.

The engineering of a more thermally stable lactate dehydrogenase by reduction of a water-accessible hydrophobic surface.
Wigley, D.B., Clarke, A.R., Dunn, C.R., Barstow, D.A., Atkinson, T., Chia, W.N., Muirhead, H. and Holbrook, J.J. (1987)
Biophys. Biochim. Acta 916, 145-148.

The greater strength of arginine:carboxylate over lysine:carboxylate ion pairs. Implications for the design of novel enzymes and drugs.
Wigley, D.B., Lyall, A, Hart, K.W. and Holbrook, J.J. (1987).
Biochem. Biophys. Res. Comm. 48, 927-9.

Hydrogen bonding to the carboxyamide of NADH is not important for catalysis in lactate dehydrogenase.
Wigley, D.B., Clarke, A.R. and Holbrook, J.J. (1987).
Protein Engineering 1, 260.

Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase.
Atkinson, T, Barstow, D.A., Chia, W.N., Clarke, A.R., Hart, K.W., Waldman, A.D.B., Wigley, D.B., Wilks, H. and Holbrook, J.J. (1987).
Biochem. Soc. Trans. 15, 991-3.

1986

Site-directed mutagenesis reveals the role of a mobile arginine residue in lactate dehydrogenase catalysis.
Clarke, A.R., Wigley, D.B., Chia, W.N., Barstow, D.A., Atkinson, T. and Holbrook, J.J. (1986).
Nature, 324, 699-702.

Cloning, expression and complete nucleotide sequence of the B.stearothermophilus L-lactate dehydrogenase gene.
Barstow, D.A., Clarke, A.R., Chia, W.N., Wigley, D.B., Sharman, A.F., Holbrook, J.J., Atkinson, T. and Minton, N.P. (1986).
Gene 46, 47-55.