2zcf

File:2zcf.gif

spinqualitylabelsall models 2zcf, resolution 1.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771

OverviewOverview

Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron, enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is, conserved in all known NHases and involved in the hydrogen-bond network, around the catalytic center, with glutamic acid or asparagine. The kcat of, alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type, respectively, but the effect of mutations on Km was not very significant., In both mutants, the alphaCys114-SOH modification appeared to be, responsible for the catalysis as in native NHase. We crystallized the, nitrosylated alphaQ90N mutant and determined its structure at a resolution, of 1.43 A. The structure was basically identical to that of native, nitrosylated NHase except for the mutated site and its vicinity. The, structural difference between native and alphaQ90N mutant NHases suggested, the importance of the hydrogen bond networks between alphaGln90 and the, iron center for the catalytic activity.

About this StructureAbout this Structure

2ZCF is a Protein complex structure of sequences from Rhodococcus erythropolis with and as ligands. Active as Nitrile hydratase, with EC number 4.2.1.84 Full crystallographic information is available from OCA.

ReferenceReference

Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771., Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M, Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455

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