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1abs

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(New page: 200px<br /><applet load="1abs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abs, resolution 1.5&Aring;" /> '''PHOTOLYSED CARBONMONO...)
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[[Image:1abs.jpg|left|200px]]<br /><applet load="1abs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1abs, resolution 1.5&Aring;" />
 
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'''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''<br />
 
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==Overview==
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==PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K==
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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.
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<StructureSection load='1abs' size='340' side='right'caption='[[1abs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1abs]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1ABS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1abs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abs OCA], [https://pdbe.org/1abs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1abs RCSB], [https://www.ebi.ac.uk/pdbsum/1abs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1abs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/1abs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1abs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1ABS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ABS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of photolysed carbonmonoxy-myoglobin., Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM, Nature. 1994 Oct 27;371(6500):808-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7935843 7935843]
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</div>
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[[Category: Physeter catodon]]
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<div class="pdbe-citations 1abs" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Berendzen, J.]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Schlichting, I.]]
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[[Category: Sweet, R.M.]]
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[[Category: CMO]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: intermediate in ligand binding]]
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[[Category: oxygen storage]]
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[[Category: respiratory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:44:39 2007''
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==See Also==
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Physeter catodon]]
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[[Category: Berendzen J]]
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[[Category: Phillips Jr GN]]
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[[Category: Schlichting I]]
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[[Category: Sweet RM]]

Current revision

PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K

PDB ID 1abs

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