Download MendeleyStructure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution.
Campeotto, I., Carr, S.B., Trinh, C.H., Nelson, A.S., Berry, A., Phillips, S.E., Pearson, A.R.(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 1088-1090
- PubMed: 19923724
- DOI: https://doi.org/10.1107/S1744309109037403
- Primary Citation of Related Structures:
2WKJ - 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.
Organizational Affiliation:
Astbury Centre for Structural Molecular Biology, University of Leeds, England.
