4usz | pdb_00004usz

Crystal structure of the first bacterial vanadium dependant iodoperoxidase

spinqualitylabelsall models 4usz, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4usz is a 1 chain structure with sequence from Zobellia galactanivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: NA, VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0LAH5_ZOBGA Publication Abstract from PubMed Vanadium haloperoxidases (VHPO) are key enzymes that oxidize halides and are involved in the biosynthesis of organo-halogens. Up to now only chloro-(VCPO) and bromoperoxidases (VBPO) have been structurally characterized, mainly from Eukaryotic species. Three putative VHPO genes were predicted in the genome of the flavobacterium Zobellia galactanivorans, a marine bacterium associated with macroalgae. In a phylogenetic analysis, these putative bacterial VHPO are closely related to other VHPO from diverse bacterial phyla, but cluster independently from eukaryotic algal VBPO and fungal VCPO. Two of these bacterial VHPO, heterogeneously produced in E. coli, were found to be strictly specific for iodide oxidation. The crystal structure of one of these vanadium-dependent iodoperoxidases, Zg-VIPO1, was solved by Multi-wavelength Anomalous Diffraction at 1.8 A, revealing a monomeric structure mainly folded into alpha-helices. This 3D structure is relatively similar to those of VCPO of the fungus Curvularia inaequalis and of Streptomyces sp., and superimposable onto the dimeric structure of algal VBPO. Surprisingly, the vanadate binding site of Zg-VIPO1 is strictly conserved with the fungal VCPO active site. Using site-directed mutagenesis we showed that specific amino-acids and the associated hydrogen-bonding network around the vanadate center are essential for the catalytic properties and also for the iodide specificity of Zg-VIPO1. Altogether, phylogeny and structure-function data support the finding that iodoperoxidase activities evolved independently in bacterial and algal lineages, and this sheds light on the evolution of the VHPO enzyme family. The Bacterial Vanadium Iodoperoxidase from the Marine Flavobacteriaceae Zobellia galactanivorans Reveals Novel Molecular and Evolutionary Features of Halide Specificity in this Enzyme Family.,Fournier JB, Rebuffet E, Delage L, Grijol R, Meslet-Cladiere L, Rzonca J, Potin P, Michel G, Czjzek M, Leblanc C Appl Environ Microbiol. 2014 Sep 26. pii: AEM.02430-14. PMID:25261522 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Haloperoxidase

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