1GTZ

Structure of STREPTOMYCES COELICOLOR TYPE II DEHYDROQUINASE R23A MUTANT IN COMPLEX WITH DEHYDROSHIKIMATE

1GTZ の概要

• エントリーDOI: 10.2210/pdb1gtz/pdb
• 関連するPDBエントリー: 1D0I 1GU0 1GU1
• 分子名称: 3-DEHYDROQUINATE DEHYDRATASE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 3-DEHYDROSHIKIMATE, ... (4 entities in total)
• 機能のキーワード: lyase, type ii dehydroquinase, shikimate pathway, dodecameric quaternary structure, tetrahedral symmetry aromatic amino acid biosynthesis
• 由来する生物種: STREPTOMYCES COELICOLOR
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 200380.24

構造登録者

Roszak, A.W.,Krell, T.,Robinson, D.A.,Hunter, I.S.,Coggins, J.R.,Lapthorn, A.J. (登録日: 2002-01-22, 公開日: 2002-06-27, 最終更新日: 2023-12-13)

主引用文献

Roszak, A.W.,Robinson, D.A.,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

実験手法

X-RAY DIFFRACTION (1.6 Å)