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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

Summary for 2WKJ
Entry DOI10.2210/pdb2wkj/pdb
Related1FDY 1FDZ 1HL2 1NAL
DescriptorN-ACETYLNEURAMINATE LYASE, PENTAETHYLENE GLYCOL, PYRUVIC ACID, ... (4 entities in total)
Functional Keywordsdirected evolution, sialic acid mimetics, lyase, aldolase, schiff base, carbohydrate metabolism, n-acetylneuraminic acid lyase
Biological sourceESCHERICHIA COLI
Total number of polymer chains4
Total formula weight134978.06
Authors
Campeotto, I.,Carr, S.B.,Trinh, C.H.,Nelson, A.S.,Berry, A.,Phillips, S.E.V.,Pearson, A.R. (deposition date: 2009-06-11, release date: 2009-12-01, Last modification date: 2023-12-13)
Primary citationCampeotto, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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数据于2025-07-09公开中

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