2v1e: Difference between revisions
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|PDB= 2v1e |SIZE=350|CAPTION= <scene name='initialview01'>2v1e</scene>, resolution 1.30Å | |PDB= 2v1e |SIZE=350|CAPTION= <scene name='initialview01'>2v1e</scene>, resolution 1.30Å | ||
|SITE= <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> | |SITE= <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> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HYD:HYDROXY+GROUP'>HYD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1azi|1AZI]], [[1bje|1BJE]], [[1dwr|1DWR]], [[1dws|1DWS]], [[1dwt|1DWT]], [[1gjn|1GJN]], [[1hrm|1HRM]], [[1hsy|1HSY]], [[1npf|1NPF]], [[1npg|1NPG]], [[1nz2|1NZ2]], [[1nz3|1NZ3]], [[1nz4|1NZ4]], [[1nz5|1NZ5]], [[1rse|1RSE]], [[1wla|1WLA]], [[1xch|1XCH]], [[1yma|1YMA]], [[1ymb|1YMB]], [[1ymc|1YMC]], [[2frf|2FRF]], [[2fri|2FRI]], [[2frj|2FRJ]], [[2frk|2FRK]], [[2in4|2IN4]], [[2v1f|2V1F]], [[2v1g|2V1G]], [[2v1h|2V1H]], [[2v1i|2V1I]], [[2v1j|2V1J]], [[2v1k|2V1K]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1e OCA], [http://www.ebi.ac.uk/pdbsum/2v1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v1e RCSB]</span> | |||
}} | }} | ||
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[[Category: Gorbitz, C H.]] | [[Category: Gorbitz, C H.]] | ||
[[Category: Hersleth, H P.]] | [[Category: Hersleth, H P.]] | ||
[[Category: ferryl]] | [[Category: ferryl]] | ||
[[Category: haem]] | [[Category: haem]] | ||
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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 Mon Mar 31 05:07:24 2008'' | ||
Revision as of 05:07, 31 March 2008
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| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , , , | ||||||
| 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, 2V1F, 2V1G, 2V1H, 2V1I, 2V1J, 2V1K
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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