2mbw

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(New page: 200px<br /><applet load="2mbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mbw, resolution 1.5&Aring;" /> '''RECOMBINANT SPERM WHA...)
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[[Image:2mbw.jpg|left|200px]]<br /><applet load="2mbw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2mbw, resolution 1.5&Aring;" />
 
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'''RECOMBINANT SPERM WHALE MYOGLOBIN (MET)'''<br />
 
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==Overview==
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==RECOMBINANT SPERM WHALE MYOGLOBIN (MET)==
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The structures of the deoxy, oxy, and aquomet forms of native sperm whale, myoglobin reconstituted with cobalt protoporphyrin IX have been determined, by x-ray crystallography. As expected, cobalt myoglobin closely resembles, native iron myoglobin in overall structure, especially in their respective, aquomet forms. In the cobalt oxymyoglobin structure, the Nepsilon of, distal histidine 64 lies within hydrogen bonding distance to both the, oxygen atom directly bonded to the cobalt and the terminal oxygen atom, in, agreement with previous EPR and resonance Raman studies. The metal atom in, cobaltous myoglobin does show a small 0.06-A out-of-porphyrin plane, displacement when moving from the oxy to deoxy state. In the case of the, native iron-containing myoglobin, the oxy to deoxy transition results in a, larger 0.16-A displacement of the metal farther out of the porphyrin, plane, attributed to an increase in spin from S = 0 to S = 2. The small, displacement in cobalt myoglobin is due to a change in coordination, geometry, not spin state (S = 1/2 for both cobalt deoxy- and, oxymyoglobin). The small out-of-porphyrin plane movement of cobalt which, accompanies deoxygenation of myoglobin also occurs in cobalt hemoglobin, and serves to explain why cooperativity, although reduced, is still, preserved when iron is replaced by cobalt in human hemoglobin.
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<StructureSection load='2mbw' size='340' side='right'caption='[[2mbw]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mbw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mbw 1mbw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBW 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=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=2mbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbw OCA], [https://pdbe.org/2mbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbw RCSB], [https://www.ebi.ac.uk/pdbsum/2mbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbw 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/mb/2mbw_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=2mbw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2MBW 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 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1MBW. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MBW OCA].
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin., Brucker EA, Olson JS, Phillips GN Jr, Dou Y, Ikeda-Saito M, J Biol Chem. 1996 Oct 11;271(41):25419-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8810310 8810310]
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[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Brucker EA]]
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[[Category: Brucker, E.A.]]
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[[Category: Phillips Jr GN]]
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[[Category: Jr., G.N.Phillips.]]
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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: respiratory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:43:32 2007''
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Current revision

RECOMBINANT SPERM WHALE MYOGLOBIN (MET)

PDB ID 2mbw

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