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2v1e
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| - | |DOMAIN= | + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01040 globin]</span> |
|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]] | |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> | |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: 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 Wed Apr 2 11:32:16 2008'' |
Revision as of 08:32, 2 April 2008
| |||||||
| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , , , | ||||||
| Domains: | globin | ||||||
| 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
| ||||||
| 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
Overview
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 Structure
2V1E is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
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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