3a16 | pdb_00003a16

Crystal Structure of Aldoxime Dehydratase (OxdRE) in Complex with Propionaldoxime

spinqualitylabelsall models 3a16, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a16 is a 4 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: HEM, MG, PXO Related: 3a15, 3a17, 3a18 Gene: oxd ("Mycobacterium erythropolis" Gray and Thornton 1928) Activity: Aliphatic aldoxime dehydratase, with EC number 4.99.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Aldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C triple bond N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 A resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 A resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE. X-ray crystal structure of michaelis complex of aldoxime dehydratase.,Sawai H, Sugimoto H, Kato Y, Asano Y, Shiro Y, Aono S J Biol Chem. 2009 Nov 13;284(46):32089-96. Epub 2009 Sep 8. PMID:19740758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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