1GU0

CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR

Summary for 1GU0

• Entry DOI: 10.2210/pdb1gu0/pdb
• Related: 1D0I 1GQN 1GQO 1GTZ 1GU1 1GUY 1GV1 1GVZ 1QFE 2DHQ
• Descriptor: 3-DEHYDROQUINATE DEHYDRATASE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: lyase, type ii dehydroquinase, shikimate pathway, dodecameric quaternary structure, tetrahedral symmetry
• Biological source: STREPTOMYCES COELICOLOR
• Total number of polymer chains: 12
• Total formula weight: 199323.83

Authors

Roszak, A.W.,Krell, T.,Robinson, D.,Hunter, I.S.,Coggins, J.R.,Lapthorn, A.J. (deposition date: 2002-01-22, release date: 2002-04-12, Last modification date: 2023-12-13)

Primary citation

Roszak, A.W.,Robinson, D.,Krell, T.,Hunter, I.S.,Fredrickson, M.,Abell, C.,Coggins, J.R.,Lapthorn, A.J.
The Structure and Mechanism of the Type II Dehydroquinase from Streptomyces Coelicolor
Structure, 10:493-, 2002

PubMed Abstract: The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high resolution in complexes with a number of ligands, including dehydroshikimate and a rationally designed transition state analogue, 2,3-anhydro-quinic acid. These structures define the active site of the enzyme and the role of key amino acid residues and provide snap shots of the catalytic cycle. The resolution of the flexible lid domain (residues 21-31) shows that the invariant residues Arg23 and Tyr28 close over the active site cleft. The tyrosine acts as the base in the initial proton abstraction, and evidence is provided that the reaction proceeds via an enol intermediate. The active site of the structure of DHQase in complex with the transition state analog also includes molecules of tartrate and glycerol, which provide a basis for further inhibitor design.

PubMed: 11937054
DOI: 10.1016/S0969-2126(02)00747-5

Experimental method

X-RAY DIFFRACTION (2 Å)