1KMJ

E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).

Summary for 1KMJ

• Entry DOI: 10.2210/pdb1kmj/pdb
• Related: 1JF9 1KMJ
• Descriptor: Selenocysteine lyase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: persulfide perselenide nifs pyridoxal phosphate, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 44759.80

Authors

Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2001-12-16, release date: 2001-12-21, Last modification date: 2023-11-15)

Primary citation

Lima, C.D.
Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation.
J.Mol.Biol., 315:1199-1208, 2002

PubMed Abstract: The Escherichia coli NifS CsdB protein is a member of the homodimeric pyridoxal 5'-phosphate (PLP)-dependent family of enzymes. These enzymes are capable of decomposing cysteine or selenocysteine into L-alanine and sulfur or selenium, respectively. E. coli NifS CsdB has a high specificity for L-selenocysteine in comparison to l-cysteine, suggesting a role for this enzyme is selenium metabolism. The 2.0 A crystal structure of E. coli NifS CsdB reveals a high-resolution view of the active site of this enzyme in apo-, persulfide, perselenide, and selenocysteine-bound intermediates, suggesting a mechanism for the stabilization of the enzyme persulfide and perselenide intermediates during catalysis, a necessary intermediate in the formation of sulfur and selenium containing metabolites.

PubMed: 11827487
DOI: 10.1006/jmbi.2001.5308

Experimental method

X-RAY DIFFRACTION (2 Å)