1ajh

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(New page: 200px<br /><applet load="1ajh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ajh, resolution 1.69&Aring;" /> '''PHOTOPRODUCT OF CARB...)
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[[Image:1ajh.gif|left|200px]]<br /><applet load="1ajh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ajh, resolution 1.69&Aring;" />
 
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'''PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K'''<br />
 
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==Overview==
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==PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K==
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Myoglobin's reversible binding of oxygen is a model for studies of protein, control of ligand binding and discrimination. Protein relaxation and, geminate ligand rebinding subsequent to ligand photodissociation have been, studied extensively by a variety of techniques. The ps to ns time scales, for these processes are still much shorter than the ms time resolution of, X-ray diffraction experiments, but it may be possible to trap these, intermediates at low temperatures. We report here an X-ray diffraction, investigation of structural changes induced by photolysis of carbonmonoxy, myoglobin crystals at 40 K. Our results provide a structural basis for the, interpretation of ambient and low temperature spectroscopic observations, and molecular dynamics simulations of the ligand photodissociation and, binding processes in haem proteins.
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<StructureSection load='1ajh' size='340' side='right'caption='[[1ajh]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ajh]] 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=1AJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AJH 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]] 1.69&#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=1ajh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ajh OCA], [https://pdbe.org/1ajh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ajh RCSB], [https://www.ebi.ac.uk/pdbsum/1ajh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ajh 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/aj/1ajh_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=1ajh 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's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.
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==About this Structure==
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Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K.,Teng TY, Srajer V, Moffat K Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074<ref>PMID:7634074</ref>
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1AJH 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=1AJH 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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Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K., Teng TY, Srajer V, Moffat K, Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7634074 7634074]
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</div>
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[[Category: Physeter catodon]]
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<div class="pdbe-citations 1ajh" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Moffat, K.]]
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[[Category: Srajer, V.]]
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[[Category: Teng, T.Y.]]
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[[Category: CMO]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: heme]]
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[[Category: oxygen transport]]
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[[Category: photoproduct intermediate]]
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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 10:54:24 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: Moffat K]]
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[[Category: Srajer V]]
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[[Category: Teng TY]]

Current revision

PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K

PDB ID 1ajh

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