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Structure paper

TitleThe narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 68, Page 909-919, Year 2012
Publish dateJul 4, 2011 (structure data deposition date)
AuthorsRaj, I. / Kumar, S. / Gourinath, S.
External linksActa Crystallogr. ,Sect. D / PubMed:22868756
MethodsX-ray diffraction
Resolution1.77 - 1.79 Å
Structure data

PDB-3spx:
Crystal structure of O-Acetyl Serine Sulfhydrylase from Leishmania donovani
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-3t4p:
Crystal structure of O-Acetyl Serine Sulfhydrylase from Leishmania donovani in complex with designed tetrapeptide
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • leishmania donovani (eukaryote)
KeywordsTRANSFERASE / O-Acetyl Serine Sulfhydrylase / Cysteine Synthase / Type II PLP dependent enzyme / Cysteine biocynthesis / Serine Acetyl Transferase / cytosolic / TRANSFERASE/TRANSFERASE INHIBITOR / The tryptophan synthase family (fold type II) / sulfhydrylase / sulfhydrylase-inhibitor complex / peptide-OASS complex / TRANSFERASE-TRANSFERASE INHIBITOR complex

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