2v1i | pdb_00002v1i

Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 6.8

spinqualitylabelsall models 2v1i, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v1i 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, SO4 Related: 1azi, 1bje, 1dwr, 1dws, 1dwt, 1gjn, 1hrm, 1hsy, 1npf, 1npg, 1nz2, 1nz3, 1nz4, 1nz5, 1rse, 1wla, 1xch, 1yma, 1ymb, 1ymc, 2frf, 2fri, 2frj, 2frk, 2in4, 2v1e, 2v1f, 2v1g, 2v1h, 2v1j, 2v1k 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 High resolution crystal structures of myoglobin in the pH range 5.2-8.7 have been used as models for the peroxide-derived compound II intermediates in heme peroxidases and oxygenases. The observed Fe-O bond length (1.86-1.90 A) is consistent with that of a single bond. The compound II state of myoglobin in crystals was controlled by single-crystal microspectrophotometry before and after synchrotron data collection. We observe some radiation-induced changes in both compound II (resulting in intermediate H) and in the resting ferric state of myoglobin. These radiation-induced states are quite unstable, and compound II and ferric myoglobin are immediately regenerated through a short heating above the glass transition temperature (<1 s) of the crystals. It is unclear how this influences our compound II structures compared with the unaffected compound II, but some crystallographic data suggest that the influence on the Fe-O bond distance is minimal. Based on our crystallographic and spectroscopic data we suggest that for myoglobin the compound II intermediate consists of an Fe(IV)-O species with a single bond. The presence of Fe(IV) is indicated by a small isomer shift of delta = 0.07 mm/s from Mossbauer spectroscopy. Earlier quantum refinements (crystallographic refinement where the molecular-mechanics potential is replaced by a quantum chemical calculation) and density functional theory calculations suggest that this intermediate H species is protonated. Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O.,Hersleth HP, Uchida T, Rohr AK, Teschner T, Schunemann V, Kitagawa T, Trautwein AX, Gorbitz CH, Andersson KK J Biol Chem. 2007 Aug 10;282(32):23372-86. Epub 2007 Jun 12. PMID:17565988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin

Proteopedia Page Contributors and Editors (what is this?)

OCA