3x24 | pdb_00003x24

Crystal structure of Nitrile Hydratase mutant bR56K complexed with Trimethylacetonitrile, photo-activated for 120 min

spinqualitylabelsall models 3x24, resolution 1.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x24 is a 2 chain structure with sequence from "mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, MG, TAN NonStd Res: CSD, CSO Related: 3wvd, 3wve, 3x20, 3x25, 3x26 Gene: nthA ("Mycobacterium erythropolis" Gray and Thornton 1928), nthB, nha2 ("Mycobacterium erythropolis" Gray and Thornton 1928) Activity: Nitrile hydratase, with EC number 4.2.1.84 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NHAA_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class. [NHAB_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Publication Abstract from PubMed 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(-) . Time-Resolved Crystallography of the Reaction Intermediate of Nitrile Hydratase: Revealing a Role for the Cysteinesulfenic Acid Ligand as a Catalytic Nucleophile.,Yamanaka Y, Kato Y, Hashimoto K, Iida K, Nagasawa K, Nakayama H, Dohmae N, Noguchi K, Noguchi T, Yohda M, Odaka M Angew Chem Int Ed Engl. 2015 Sep 7;54(37):10763-7. doi: 10.1002/anie.201502731. PMID:26333053 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitrile hydratase

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