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Structure paper

TitleCrystallographic study to determine the substrate specificity of an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway
Journal, issue, pagesJ. Bacteriol., Vol. 195, Page 1741-1749, Year 2013
Publish dateJul 26, 2012 (structure data deposition date)
AuthorsOda, K. / Matoba, Y. / Kumagai, T. / Noda, M. / Sugiyama, M.
External linksJ. Bacteriol. / PubMed:23396912
MethodsX-ray diffraction
Resolution1.7 - 1.81 Å
Structure data

PDB-3vvl:
Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-3vvm:
Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • streptomyces lavendulae subsp. lavendulae (bacteria)
KeywordsTRANSFERASE / D-cycloserine / alpha/beta hydrolase domain / L-serine-O-acetyltransferase

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