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1mni

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(New page: 200px<br /><applet load="1mni" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mni, resolution 2.07&Aring;" /> '''ALTERATION OF AXIAL ...)
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[[Image:1mni.jpg|left|200px]]<br /><applet load="1mni" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mni, resolution 2.07&Aring;" />
 
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'''ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT'''<br />
 
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==Overview==
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==ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT==
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Pig and human myoglobin have been engineered to reverse the positions of, the distal histidine and valine (i.e. His64(E7)--&gt;Val and, Val68(E11)--&gt;His). Spectroscopic and ligand binding properties have been, measured for human and pig H64V/V68H myoglobin, and the structure of the, pig H64V/V68H double mutant has been determined to 2.07-A resolution by, x-ray crystallography. The crystal structure shows that the N epsilon of, His68 is located 2.3 A away from the heme iron, resulting in the formation, of a hexacoordinate species. The imidazole plane of His68 is tilted, relative to the heme normal; moreover it is not parallel to that of His93, in agreement with our previous proposal (Qin, J., La Mar, G. N., Dou, Y., Admiraal, S. J., and Ikeda-Saito, M. (1994) J. Biol. Chem. 269, 1083-1090). At cryogenic temperatures, the heme iron is in a low spin, state, which exhibits a highly anisotropic EPR spectrum (g1 = 3.34, g2 =, 2.0, and g3 &lt; 1), quite different from that of the imidazole complex of, metmyoglobin. The mean iron-nitrogen distance is 2.01 A for the low spin, ferric state as determined by x-ray spectroscopy. The ferrous form of, H64V/V68H myoglobin shows an optical spectrum that is similar to that of, b-type cytochromes and consistent with the hexacoordinate bisimidazole, hemin structure determined by the x-ray crystallography. The double, mutation lowers the ferric/ferrous couple midpoint potential from +54 mV, of the wild-type protein to -128 mV. Ferrous H64V/V68H myoglobin binds CO, and NO to form stable complexes, but its reaction with O2 results in a, rapid autooxidation to the ferric species. All of these results, demonstrate that the three-dimensional positions of His64 and Val68 in the, wild-type myoglobin are as important as the chemical nature of the side, chains in facilitating reversible O2 binding and inhibiting autooxidation.
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<StructureSection load='1mni' size='340' side='right'caption='[[1mni]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mni]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MNI 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]] 2.07&#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></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=1mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mni OCA], [https://pdbe.org/1mni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mni RCSB], [https://www.ebi.ac.uk/pdbsum/1mni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mni ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_PIG MYG_PIG] 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/mn/1mni_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=1mni 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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1MNI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MNI 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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Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64--&gt;Val/Val68--&gt;His double mutant., Dou Y, Admiraal SJ, Ikeda-Saito M, Krzywda S, Wilkinson AJ, Li T, Olson JS, Prince RC, Pickering IJ, George GN, J Biol Chem. 1995 Jul 7;270(27):15993-6001. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7608158 7608158]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Krzywda, S.]]
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[[Category: Krzywda S]]
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[[Category: Wilkinson, A.J.]]
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[[Category: Wilkinson AJ]]
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[[Category: HEM]]
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[[Category: oxygen storage]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:33:20 2007''
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Current revision

ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT

PDB ID 1mni

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