4n2x | pdb_00004n2x

Crystal Structure of DL-2-haloacid dehalogenase

spinqualitylabelsall models 4n2x, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n2x is a 6 chain structure with sequence from Methylobacterium sp. cpa1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: dl-dex (Methylobacterium sp. CPA1) Activity: 2-haloacid dehalogenase (configuration-inverting), with EC number 3.8.1.10 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step. Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.,Siwek A, Omi R, Hirotsu K, Jitsumori K, Esaki N, Kurihara T, Paneth P Arch Biochem Biophys. 2013 Sep 23;540(1-2):26-32. doi: 10.1016/j.abb.2013.09.012. PMID:24071515 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dehalogenase

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