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Structure paper

TitleSnapshots of the Cystine Lyase "C-DES" during Catalysis: Studies in Solution and in the Crystalline State
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 357-365, Year 2003
Publish dateOct 24, 2002 (structure data deposition date)
AuthorsKaiser, J.T. / Bruno, S. / Clausen, T. / Huber, R. / Schiaretti, F. / Mozzarelli, A. / Kessler, D.
External linksJ. Biol. Chem. / PubMed:12386155
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-1n2t:
C-DES Mutant K223A with GLY Covalenty Linked to the PLP-cofactor
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1n31:
Structure of A Catalytically Inactive Mutant (K223A) of C-DES with a Substrate (Cystine) Linked to the Co-Factor
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-GLY:
GLYCINE

ChemComp-HOH:
WATER

ChemComp-CYS:
CYSTEINE

Source
  • synechocystis sp. pcc 6714 (bacteria)
KeywordsLYASE / FES CLUSTER BIOSYNTHESIS / NIFS / PYRIDOXAL 5'-PHOSPHATE / INACTIVE MUTANT / substrate complex / FE-S cluster synthesis / NifS-like

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