1bzr

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(New page: 200px<br /><applet load="1bzr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bzr, resolution 1.15&Aring;" /> '''ATOMIC RESOLUTION CR...)
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[[Image:1bzr.jpg|left|200px]]<br /><applet load="1bzr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bzr, resolution 1.15&Aring;" />
 
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'''ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''<br />
 
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==Overview==
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==ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE==
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The crystal structures of myoglobin in the deoxy- and carbon, monoxide-ligated states at a resolution of 1.15 angstroms show that carbon, monoxide binding at ambient temperatures requires concerted motions of the, heme, the iron, and helices E and F for relief of steric inhibition. These, steps constitute the main mechanism by which heme proteins lower the, affinity of the heme group for the toxic ligand carbon monoxide.
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<StructureSection load='1bzr' size='340' side='right'caption='[[1bzr]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bzr]] 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=1BZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BZR 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]] 1.15&#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=1bzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bzr OCA], [https://pdbe.org/1bzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bzr RCSB], [https://www.ebi.ac.uk/pdbsum/1bzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bzr 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/bz/1bzr_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=1bzr 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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The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
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==About this Structure==
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A steric mechanism for inhibition of CO binding to heme proteins.,Kachalova GS, Popov AN, Bartunik HD Science. 1999 Apr 16;284(5413):473-6. PMID:10205052<ref>PMID:10205052</ref>
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1BZR 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=1BZR 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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A steric mechanism for inhibition of CO binding to heme proteins., Kachalova GS, Popov AN, Bartunik HD, Science. 1999 Apr 16;284(5413):473-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10205052 10205052]
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</div>
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[[Category: Physeter catodon]]
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<div class="pdbe-citations 1bzr" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Bartunik, H.D.]]
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[[Category: Kachalova, G.S.]]
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[[Category: Popov, A.N.]]
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[[Category: CMO]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: atomic resolution]]
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[[Category: carbonmonoxy myoglobin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:02:49 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: Bartunik HD]]
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[[Category: Kachalova GS]]
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[[Category: Popov AN]]

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ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE

PDB ID 1bzr

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