2WKJ

Crystal structure of the E192N mutant of E. Coli N-acetylneuraminic acid lyase in complex with pyruvate at 1.45A resolution in space group P212121

2WKJ の概要

• エントリーDOI: 10.2210/pdb2wkj/pdb
• 関連するPDBエントリー: 1FDY 1FDZ 1HL2 1NAL
• 分子名称: N-ACETYLNEURAMINATE LYASE, PENTAETHYLENE GLYCOL, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: directed evolution, sialic acid mimetics, lyase, aldolase, schiff base, carbohydrate metabolism, n-acetylneuraminic acid lyase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 134978.06

構造登録者

Campeotto, I.,Carr, S.B.,Trinh, C.H.,Nelson, A.S.,Berry, A.,Phillips, S.E.V.,Pearson, A.R. (登録日: 2009-06-11, 公開日: 2009-12-01, 最終更新日: 2023-12-13)

主引用文献

Campeotto, I.,Carr, S.B.,Trinh, C.H.,Nelson, A.S.,Berry, A.,Phillips, S.E.,Pearson, A.R.
Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 65:1088-1090, 2009

PubMed Abstract: The structure of a mutant variant of Escherichia coli N-acetyl-d-neuraminic acid lyase (NAL), E192N, in complex with pyruvate has been determined in a new crystal form. It crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 78.3, b = 108.5, c = 148.3 angstrom. Pyruvate has been trapped in the active site as a Schiff base with the catalytic lysine (Lys165) without the need for reduction. Unlike the previously published crystallization conditions for the wild-type enzyme, in which a mother-liquor-derived sulfate ion is strongly bound in the catalytic pocket, the low-salt conditions described here will facilitate the determination of further E. coli NAL structures in complex with other activesite ligands.

PubMed: 19923724
DOI: 10.1107/S1744309109037403

実験手法

X-RAY DIFFRACTION (1.45 Å)