1abs
From Proteopedia
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| - | [[ | + | ==PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K== |
| + | <StructureSection load='1abs' size='340' side='right' caption='[[1abs]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1abs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ABS FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <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=1abs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1abs RCSB], [http://www.ebi.ac.uk/pdbsum/1abs 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/ab/1abs_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 == | ||
| + | Myoglobin is a globular haem protein that reversibly binds ligands such as O2 and CO. Single photons of visible light can break the covalent bond between CO and the haem iron in carbon-monoxy-myoglobin (MbCO) and thus form an unstable intermediate, Mb*CO, with the CO inside the protein. The ensuing rebinding process has been extensively studied as a model for the interplay of dynamics, structure and function in protein reactions. We have used X-ray crystallography at liquid-helium temperatures to determine the structure of Mb*CO to a resolution of 1.5 A. The photodissociated CO lies on top of the haem pyrrole ring C. Comparison with the CO-bound and unligated myoglobin structures reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haem plane, the iron-proximal histidine bonds is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket. | ||
| - | + | Crystal structure of photolysed carbonmonoxy-myoglobin.,Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM Nature. 1994 Oct 27;371(6500):808-12. PMID:7935843<ref>PMID:7935843</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Myoglobin|Myoglobin]] | *[[Myoglobin|Myoglobin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Berendzen, J.]] | [[Category: Berendzen, J.]] | ||
Revision as of 08:29, 23 July 2014
PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K
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