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TitleThe Reaction Mechanism of N-Acetylneuraminic Acid Lyase Revealed by a Combination of Crystallography, Qm/Mm Simulation and Mutagenesis.
Journal, issue, pagesAcs Chem. Biol., Vol. 9, Page 1025-, Year 2014
Publish dateJul 3, 2013 (structure data deposition date)
AuthorsDaniels, A.D. / Campeotto, I. / Van Der Kamp, M.W. / Bolt, A.H. / Trinh, C.H. / Phillips, S.E.V. / Pearson, A.R. / Nelson, A. / Mulholland, A.J. / Berry, A.
External linksAcs Chem. Biol. / PubMed:24521460
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-4bwl:
Structure of the Y137A mutant of E. coli N-acetylneuraminic acid lyase in complex with pyruvate, N-acetyl-D-mannosamine and N- acetylneuraminic acid
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SI3:
5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-2-ulosonic acid

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-MN9:
2-(ACETYLAMINO)-2-DEOXY-D-MANNOSE

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsLYASE / DIRECTED EVOLUTION / SUBSTRATE SPECIFICITY / PROTEIN ENGINEERING

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