3qpi

Crystal Structure of Dimeric Chlorite Dismutases from Nitrobacter winogradskyi

spinqualitylabelsall models 3qpi, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qpi is a 2 chain structure with sequence from Nitwn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Gene: Nwi_2442 (NITWN) Activity: Chlorite O(2)-lyase, with EC number 1.13.11.49 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Chlorite dismutase (Cld) is a unique heme enzyme catalyzing the conversion of ClO(2)(-) to Cl(-) and O(2). Cld is usually found in perchlorate- or chlorate-reducing bacteria but was also recently identified in a nitrite-oxidizing bacterium of the genus Nitrospira. Here we characterized a novel Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi which is significantly smaller than all previously known chlorite dismutases. Its three-dimensional (3D) crystal structure revealed a dimer of two identical subunits, which sharply contrasts with the penta- or hexameric structures of other chlorite dismutases. Despite a truncated N-terminal domain in each subunit, this novel enzyme turned out to be a highly efficient chlorite dismutase (K(m) = 90 muM; k(cat) = 190 s(-1); k(cat)/K(m) = 2.1 x 10(6) M(-1) s(-1)), demonstrating a greater structural and phylogenetic diversity of these enzymes than was previously known. Based on comparative analyses of Cld sequences and 3D structures, signature amino acid residues that can be employed to assess whether uncharacterized Cld-like proteins may have a high chlorite-dismutating activity were identified. Interestingly, proteins that contain all these signatures and are phylogenetically closely related to the novel-type Cld of N. winogradskyi exist in a large number of other microbes, including other nitrite oxidizers. Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi.,Mlynek G, Sjoblom B, Kostan J, Fureder S, Maixner F, Gysel K, Furtmuller PG, Obinger C, Wagner M, Daims H, Djinovic-Carugo K J Bacteriol. 2011 May;193(10):2408-17. Epub 2011 Mar 25. PMID:21441524 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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