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Structure paper

TitleLeishmania Trypanothione Synthetase-Amidase Structure Reveals a Basis for Regulation of Conflicting Synthetic and Hydrolytic Activities.
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 17672-, Year 2008
Publish dateFeb 13, 2008 (structure data deposition date)
AuthorsFyfe, P.K. / Oza, S.L. / Fairlamb, A.H. / Hunter, W.N.
External linksJ. Biol. Chem. / PubMed:18420578
MethodsX-ray diffraction
Resolution2.3 - 2.8 Å
Structure data

PDB-2vob:
TRYPANOTHIONE SYNTHETASE
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2vpm:
Trypanothione synthetase
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-2vps:
Structure Of The Bifunctional Leishmania Major Trypanothione Synthetase-Amidase
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-BR:
BROMIDE ION

Source
  • leishmania major (eukaryote)
KeywordsLIGASE

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