2v1e: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2v1e.png|left|200px]]
+==CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II - INTERMEDIATE H AT PH 6.8==
+<StructureSection load='2v1e' size='340' side='right' caption='[[2v1e]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2v1e]] 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=2V1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V1E FirstGlance]. <br>
+</td></tr><tr><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=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+<tr><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]], [[2v1f|2v1f]], [[2v1g|2v1g]], [[2v1h|2v1h]], [[2v1i|2v1i]], [[2v1j|2v1j]], [[2v1k|2v1k]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2v1e RCSB], [http://www.ebi.ac.uk/pdbsum/2v1e PDBsum]</span></td></tr>
+<table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v1e_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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 (&lt;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.
-{{STRUCTURE_2v1e|  PDB=2v1e  |  SCENE=  }}
+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<ref>PMID:17565988</ref>
-===CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II - INTERMEDIATE H AT PH 6.8===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_17565988}}
-==About this Structure==
-[[2v1e]] 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=2V1E OCA].
 ==See Also==
 *[[Myoglobin|Myoglobin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017565988</ref><ref group="xtra">PMID:011935353</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Equus caballus]]
 [[Category: Andersson, K K.]]