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TitleCrystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase.
Journal, issue, pagesProteins, Vol. 72, Page 1222-1232, Year 2008
Publish dateMay 2, 2007 (structure data deposition date)
AuthorsChinthalapudi, K. / Kumar, M. / Kumar, S. / Jain, S. / Alam, N. / Gourinath, S.
External linksProteins / PubMed:18350570
MethodsX-ray diffraction
Resolution1.86 - 2.4 Å
Structure data

PDB-2pqm:
Crystal structure of Cysteine Synthase (OASS) from Entamoeba histolytica at 1.86 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-3bm5:
Crystal structure of O-acetyl-serine sulfhydrylase from Entamoeba histolytica in complex with cysteine
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-CYS:
CYSTEINE

Source
  • entamoeba histolytica (eukaryote)
  • entamoeba histolytica hm-1:imss (eukaryote)
KeywordsLYASE / OASS / Cysteine synthase / PLP / LYASE/BIOSYNTHETIC PROTEIN / Cys-OASS complex / domain movement / Pyridoxal phosphate / LYASE-BIOSYNTHETIC PROTEIN COMPLEX

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