2QJI

M. jannaschii ADH synthase complexed with dihydroxyacetone phosphate and glycerol

2QJI の概要

• エントリーDOI: 10.2210/pdb2qji/pdb
• 関連するPDBエントリー: 2QJG 2QJH
• 分子名称: Putative aldolase MJ0400, 1,3-DIHYDROXYACETONEPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-alpha barrel, lyase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 599626.68

構造登録者

Ealick, S.E.,Morar, M. (登録日: 2007-07-07, 公開日: 2007-10-30, 最終更新日: 2024-10-30)

主引用文献

Morar, M.,White, R.H.,Ealick, S.E.
Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids.
Biochemistry, 46:10562-10571, 2007

PubMed Abstract: Genes responsible for the generation of 3-dehydroquinate (DHQ), an early metabolite in the established shikimic pathway of aromatic amino acid biosynthesis, are absent in most euryarchaeotes. Alternative gene products, Mj0400 and Mj1249, have been identified in Methanocaldococcus jannaschii as the enzymes involved in the synthesis of DHQ. 2-Amino-3,7-dideoxy-d-threo-hept-6-ulosonic acid (ADH) synthase, the product of the Mj0400 gene, catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate and l-aspartate semialdehyde to yield ADH. Dehydroquinate synthase II, the product of the Mj1249 gene, then catalyzes deamination and cyclization of ADH, resulting in DHQ, which is fed into the canonical pathway. Three crystal structures of ADH synthase were determined in this work: a complex with a substrate analogue, fructose 1,6-bisphosphate, a complex with dihydroxyacetone phosphate (DHAP), thought to be a product of fructose 1-phosphate cleavage, and a native structure containing copurified ligands, modeled as DHAP and glycerol. On the basis of the structural analysis and comparison of the enzyme with related aldolases, ADH synthase is classified as a new member of the class I aldolase superfamily. The description of the active site allows for the identification and characterization of possible catalytic residues, Lys184, which is responsible for formation of the Schiff base intermediate, and Asp33 and Tyr153, which are candidates for the general acid/base catalysis.

PubMed: 17713928
DOI: 10.1021/bi700934v

実験手法

X-RAY DIFFRACTION (2.8 Å)