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Structure paper

TitleStructures of enzyme-intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 69, Page 1470-1481, Year 2013
Publish dateSep 18, 2012 (structure data deposition date)
AuthorsLiu, H. / Gao, Y. / Zhang, M. / Qiu, X. / Cooper, A.J.L. / Niu, L. / Teng, M.
External linksActa Crystallogr. ,Sect. D / PubMed:23897470
MethodsX-ray diffraction
Resolution1.91 - 2.04 Å
Structure data

PDB-4h5u:
Structural insights into yeast Nit2: wild-type yeast Nit2
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-4hg3:
Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-4hg5:
Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

PDB-4hgd:
Structural insights into yeast Nit2: C169S mutant of yeast Nit2 in complex with an endogenous peptide-like ligand
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-CAC:
CACODYLATE ION

ChemComp-HOH:
WATER

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-OAA:
OXALOACETATE ION

ChemComp-KGT:
N-(4-carboxy-4-oxobutanoyl)-L-cysteinylglycine

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsHYDROLASE / similar to mouse Nit2 / probable CN hydolase / nitrilase superfamily / omega-amidase

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