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2v1j

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Revision as of 10:40, 7 July 2021

Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 8.7

Structural highlights

2v1j 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:	, ,
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, 2v1i, 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hersleth HP, Uchida T, Rohr AK, Teschner T, Schunemann V, Kitagawa T, Trautwein AX, Gorbitz CH, Andersson KK. Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O. J Biol Chem. 2007 Aug 10;282(32):23372-86. Epub 2007 Jun 12. PMID:17565988 doi:10.1074/jbc.M701948200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v1j"

@@ Line 3: / Line 3: @@
 <StructureSection load='2v1j' size='340' side='right'caption='[[2v1j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v1j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V1J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]], [[2v1e|2v1e]], [[2v1f|2v1f]], [[2v1g|2v1g]], [[2v1h|2v1h]], [[2v1i|2v1i]], [[2v1k|2v1k]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]], [[2v1e|2v1e]], [[2v1f|2v1f]], [[2v1g|2v1g]], [[2v1h|2v1h]], [[2v1i|2v1i]], [[2v1k|2v1k]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1j OCA], [http://pdbe.org/2v1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v1j RCSB], [http://www.ebi.ac.uk/pdbsum/2v1j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1j ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1j OCA], [https://pdbe.org/2v1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1j RCSB], [https://www.ebi.ac.uk/pdbsum/2v1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Myoglobin|Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 == References ==
 <references/>

2v1j

From Proteopedia

Revision as of 10:40, 7 July 2021

Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 8.7

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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