3WVD: Crystal Structure Of Nitrile Hydratase Mutant Br56k Complexed With Trimethylacetonitrile, Photo-activated For 50 Min

Citation:
Abstract
The reaction mechanism of nitrile hydratase (NHase) was investigated using time-resolved crystallography of the mutant NHase, in which betaArg56, strictly conserved and hydrogen bonded to the two post-translationally oxidized cysteine ligands, was replaced by lysine, and pivalonitrile was the substrate. The crystal structures of the reaction intermediates were determined at high resolution (1.2-1.3 A). In combination with FTIR analyses of NHase following hydration in H2 (18) O, we propose that the metal-coordinated substrate is nucleophilically attacked by the O(SO(-) ) atom of alphaCys114-SO(-) , followed by nucleophilic attack of the S(SO(-) ) atom by a betaArg56-activated water molecule to release the product amide and regenerate alphaCys114-SO(-) .
PDB ID: 3WVDDownload
MMDB ID: 130036
PDB Deposition Date: 2014/5/17
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.18  Å
Source Organism:
Similar Structures:
Biological Unit for 3WVD: dimeric; determined by author and by software (PISA)
Molecular Components in 3WVD
Label Count Molecule
Proteins (2 molecules)
1
Nitrile Hydratase Subunit Alpha
Molecule annotation
1
Nitrile Hydratase Subunit Beta
Molecule annotation
Chemicals (5 molecules)
1
1
2
3
3
1
* Click molecule labels to explore molecular sequence information.

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