2zcf

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spinqualitylabelsall models PDB ID 2zcf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.43Å
Ligands:	and
Gene:	nthA (Rhodococcus erythropolis), nthB (Rhodococcus erythropolis)
Activity:	Nitrile hydratase, with EC number 4.2.1.84
Coordinates:	save as pdb, mmCIF, xml

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

Overview

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 Structure

2ZCF is a Protein complex structure of sequences from Rhodococcus erythropolis. Full crystallographic information is available from OCA.

Reference

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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