2vlz

Crystal structure of peroxymyoglobin generated by cryoradiolytic reduction of myoglobin compound III

spinqualitylabelsall models 2vlz, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vlz is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, HEM, PEO, PER, SO4 Related: 1bje, 2in4, 1nz3, 2v1i, 2v1f, 1dws, 1hsy, 2v1g, 1npg, 1rse, 1nz5, 2v1k, 1ymc, 1wla, 2frj, 1npf, 1nz4, 1dwr, 1nz2, 1ymb, 2frf, 1dwt, 2frk, 2v1h, 2fri, 1xch, 1yma, 1gjn, 1hrm, 2v1j, 2v1e, 1azi, 2vly, 2vm0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. 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 Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallographic data collection. We have generated and solved the 1.30 A (1 A=0.1 nm) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe-O distance of 1.8 A and O-O bond of 1.3 A in accordance with a Fe(II)-O-O- (or Fe(III)-O-O2-) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metalloproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O-O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction. The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection.,Hersleth HP, Hsiao YW, Ryde U, Gorbitz CH, Andersson KK Biochem J. 2008 Jun 1;412(2):257-64. PMID:18215120 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin 3D structures

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