We are studying two enzymes from the shikimate pathway, dehydroquinate synthase (DHQS) and 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS). Both enzymes have been the subject of numerous studies to elucidate their reaction mechanisms. Crystal structures of DHQS and EPSPS in the presence and absence of substrates, cofactors and/or inhibitors are now available. These structures reveal movements of domains, rearrangements of loops and changes in side-chain positions necessary for the formation of a catalytically competent active site. The potential for using complementary small-angle X-ray scattering (SAXS) studies to confirm the presence of these structural differences in solution has also been explored. Comparative analysis of crystal structures, in the presence and absence of ligands, has revealed structural features critical for substrate-binding and catalysis. We have also analysed these structures by generating GRID energy maps to detect favourable binding sites. The combination of X-ray crystallography, SAXS and computational techniques provides an enhanced analysis of structural features important for the function of these complex enzymes.
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Conference Article|
June 01 2003
Twists and turns: a tale of two shikimate-pathway enzymes
K.A. Brown;
K.A. Brown
1
*Department of Biological Sciences, CMMI, Flowers Building, Imperial College, London SW7 2AY, U.K.
1To whom correspondence should be addressed (e-mail k.brown@ic.ac.uk).
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E.P. Carpenter;
E.P. Carpenter
*Department of Biological Sciences, CMMI, Flowers Building, Imperial College, London SW7 2AY, U.K.
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K.A. Watson;
K.A. Watson
†The BioCentre, University of Reading, Reading RG6 6AS, U.K.
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J.R. Coggins;
J.R. Coggins
‡Division of Biochemistry and Molecular Biology, Institute of Biomedical Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, U.K.
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A.R. Hawkins;
A.R. Hawkins
§Department of Biochemistry and Genetics, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, U.K.
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M.H.J. Koch;
M.H.J. Koch
∥European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, 22603 Hamburg, Germany
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D.I. Svergun
D.I. Svergun
∥European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, 22603 Hamburg, Germany
¶Institute of Crystallography, Russian Academy of Sciences, 117333 Moscow, Russia
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (3): 543–547.
Citation
K.A. Brown, E.P. Carpenter, K.A. Watson, J.R. Coggins, A.R. Hawkins, M.H.J. Koch, D.I. Svergun; Twists and turns: a tale of two shikimate-pathway enzymes. Biochem Soc Trans 1 June 2003; 31 (3): 543–547. doi: https://doi.org/10.1042/bst0310543
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