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Structure paper

TitleStructural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 3076-3085, Year 2009
Publish dateOct 23, 2006 (structure data deposition date)
AuthorsSun, Q. / Collins, R. / Huang, S. / Holmberg-Schiavone, L. / Anand, G.S. / Tan, C.-H. / van-den-Berg, S. / Deng, L.-W. / Moore, P.K. / Karlberg, T. / Sivaraman, J.
External linksJ. Biol. Chem. / PubMed:19019829
MethodsX-ray diffraction
Resolution2 - 2.6 Å
Structure data

PDB-2nmp:
Crystal structure of human Cystathionine gamma lyase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3cog:
Crystal structure of human cystathionase (Cystathionine gamma lyase) in complex with DL-propargylglycine
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3elp:
Structure of cystationine gamma lyase
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-NO3:
NITRATE ION

ChemComp-2AG:
(2S)-2-aminopent-4-enoic acid / inhibitor*YM

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • homo sapiens (human)
KeywordsLYASE / amino-acid biosynthesis / pyridoxal phopshate / structural genomics / Structural Genomics Consortium / SGC / CTH / PLP / Propargylglycine / inhibitor / SGC Stockholm / Cysteine biosynthesis / Disease mutation / Phosphoprotein / Pyridoxal phosphate / alpha beta protein / Alternative splicing / Cytoplasm / Polymorphism

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