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PDBsum entry 2olo
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Oxidoreductase
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PDB id
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2olo
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References listed in PDB file
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Key reference
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Title
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Nikd, An unusual amino acid oxidase essential for nikkomycin biosynthesis: structures of closed and open forms at 1.15 and 1.90 a resolution.
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Authors
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C.J.Carrell,
R.C.Bruckner,
D.Venci,
G.Zhao,
M.S.Jorns,
F.S.Mathews.
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Ref.
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Structure, 2007,
15,
928-941.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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NikD is an unusual amino-acid-oxidizing enzyme that contains covalently bound
FAD, catalyzes a 4-electron oxidation of piperideine-2-carboxylic acid to
picolinate, and plays a critical role in the biosynthesis of nikkomycin
antibiotics. Crystal structures of closed and open forms of nikD, a two-domain
enzyme, have been determined to resolutions of 1.15 and 1.9 A, respectively. The
two forms differ by an 11 degrees rotation of the catalytic domain with respect
to the FAD-binding domain. The active site is inaccessible to solvent in the
closed form; an endogenous ligand, believed to be picolinate, is bound close to
and parallel with the flavin ring, an orientation compatible with redox
catalysis. The active site is solvent accessible in the open form, but the
picolinate ligand is approximately perpendicular to the flavin ring and a
tryptophan is stacked above the flavin ring. NikD also contains a mobile cation
binding loop.
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