1iop

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(New page: 200px<br /><applet load="1iop" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iop, resolution 1.9&Aring;" /> '''INCORPORATION OF A HE...)
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[[Image:1iop.gif|left|200px]]<br /><applet load="1iop" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iop, resolution 1.9&Aring;" />
 
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'''INCORPORATION OF A HEMIN WITH THE SHORTEST ACID SIDE-CHAINS INTO MYOGLOBIN'''<br />
 
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==Overview==
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==INCORPORATION OF A HEMIN WITH THE SHORTEST ACID SIDE-CHAINS INTO MYOGLOBIN==
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Myoglobin was reconstituted with 6,7-dicarboxy-1,2,3,4,5, 8-hexamethylheme, a compact synthetic heme with the shortest acid side, chains, to pursue the structural and functional consequences after, intensive disruption of the heme propionate-apoglobin linkages in the, native protein. The electron-withdrawing carboxylate groups directly, attached to the porphyrin ring lowered the oxygen affinity by 3-fold as, compared with native myoglobin. Autoxidation of the oxy derivative to the, ferric protein proceeded with 1.6 x 10(-)2 min-1 at pH 7.0 and 30 degrees, C. The crystallographic structure of the cyanomet myoglobin with 1.9 A, resolution shows that the heme adopts a unique orientation in the protein, pocket to extend the two carboxylates toward solvent sphere. The native, globin fold is conserved, and the conformations of globin side chains are, almost intact except for those located nearby the heme 6,7-carboxylates., The 7-carboxylate only weakly interacts with Ser92 and His97 through two, mediating water molecules. The 6-carboxylate, on the other hand, forms a, novel salt bridge with Arg45 owing to conformational flexibility of the, guanidinium side chain. The proton NMR shows that the small heme does not, fluctuate about the iron-histidine bond even at 55 degreesC, suggesting, that the salt bridge between Arg45 and heme 6-carboxylate is of critical, importance to recognize and fix the heme in myoglobin.
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<StructureSection load='1iop' size='340' side='right'caption='[[1iop]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iop]] 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=1IOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOP 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]] 1.9&#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=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HE6:6,7-DICARBOXYL-1,2,3,4,5,8-HEXAMETHYLHEMIN'>HE6</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=1iop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iop OCA], [https://pdbe.org/1iop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iop RCSB], [https://www.ebi.ac.uk/pdbsum/1iop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iop 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/io/1iop_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=1iop 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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1IOP 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 CYN, SO4 and HE6 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IOP 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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Structure and function of 6,7-dicarboxyheme-substituted myoglobin., Neya S, Funasaki N, Igarashi N, Ikezaki A, Sato T, Imai K, Tanaka N, Biochemistry. 1998 Apr 21;37(16):5487-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9548931 9548931]
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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: Funasaki N]]
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[[Category: Funasaki, N.]]
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[[Category: Igarashi N]]
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[[Category: Igarashi, N.]]
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[[Category: Neya S]]
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[[Category: Neya, S.]]
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[[Category: Tanaka N]]
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[[Category: Tanaka, N.]]
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[[Category: CYN]]
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[[Category: HE6]]
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[[Category: SO4]]
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[[Category: globin fold]]
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[[Category: oxygen transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:33:02 2007''
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Current revision

INCORPORATION OF A HEMIN WITH THE SHORTEST ACID SIDE-CHAINS INTO MYOGLOBIN

PDB ID 1iop

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