2v1e: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2V1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=HYD:'>HYD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hem Binding Site For Residue A 1154'>AC1</scene>, <scene name='pdbsite=AC2:Hyd Binding Site For Residue A 1155'>AC2</scene>, <scene name='pdbsite=AC3:So4 Binding Site For Residue A 1156'>AC3</scene>, <scene name='pdbsite=AC4:So4 Binding Site For Residue A 1157'>AC4</scene>, <scene name='pdbsite=AC5:Gol Binding Site For Residue A 1158'>AC5</scene>, <scene name='pdbsite=AC6:Gol Binding Site For Residue A 1159'>AC6</scene> and <scene name='pdbsite=AC7:Gol Binding Site For Residue A 1160'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1E OCA]. | 2V1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=HYD:'>HYD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hem+Binding+Site+For+Residue+A+1154'>AC1</scene>, <scene name='pdbsite=AC2:Hyd+Binding+Site+For+Residue+A+1155'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+1156'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+1157'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+A+1158'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+A+1159'>AC6</scene> and <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+A+1160'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1E OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:49:14 2008'' |
Revision as of 11:49, 3 February 2008
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CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8
OverviewOverview
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.
About this StructureAbout this Structure
2V1E is a Single protein structure of sequence from Equus caballus with , , and as ligands. Known structural/functional Sites: , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
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
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