2vxh

The crystal structure of chlorite dismutase: a detox enzyme producing molecular oxygen

spinqualitylabelsall models 2vxh, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vxh is a 6 chain structure with sequence from Azospira oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CO3, HEM, SCN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E2DI02_9RHOO 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 Chlorite dismutase (Cld) is a key enzyme of perchlorate and chlorate respiration. This heme-based protein reduces the toxic compound chlorite into the innocuous chloride anion in a very efficient way while producing molecular oxygen. A sequence comparison between Cld homologues shows a highly conserved family. The crystal structure of Azospira oryzae strain GR-1 Cld is reported to 2.1 A resolution. The structure reveals a hexameric organization of the Cld, while each monomer exhibits a ferredoxin-like fold. The six subunits are organized in a ring structure with a maximal diameter of 9 nm and an inner diameter of 2 nm. The heme active-site pocket is solvent accessible both from the inside and the outside of the ring. Moreover, a second anion binding site that could accommodate the assumed reaction intermediate ClO(-) for further transformation has been identified near the active site. The environment of the heme cofactor was investigated with electron paramagnetic resonance spectroscopy. Apart from the high-spin ferric signal of the five-coordinate resting-state enzyme, two low-spin signals were found corresponding to six-coordinate species. The current crystal structure confirms and complements a recently proposed catalytic mechanism that proceeds via a ferryl species and a ClO(-) anion. Our structural data exclude cooperativity between the iron centers. Crystal structure of chlorite dismutase, a detoxifying enzyme producing molecular oxygen.,de Geus DC, Thomassen EA, Hagedoorn PL, Pannu NS, van Duijn E, Abrahams JP J Mol Biol. 2009 Mar 20;387(1):192-206. Epub 2009 Jan 27. PMID:19361444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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