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1mni

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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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Retrieved from "http://52.214.119.220/wiki/index.php/1mni"

Categories: Large Structures | Sus scrofa | Krzywda S | Wilkinson AJ

@@ Line 1: / Line 1: @@
-[[Image:1mni.jpg|left|200px]]
- {{Structure
+==ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT==
-|PDB= 1mni |SIZE=350|CAPTION= <scene name='initialview01'>1mni</scene>, resolution 2.07&Aring;
+<StructureSection load='1mni' size='340' side='right'caption='[[1mni]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mni OCA], [http://www.ebi.ac.uk/pdbsum/1mni PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mni RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/MYG_PIG MYG_PIG] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mni_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
-'''ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT'''
+==See Also==
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-MNI is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/7608158 7608158]
-[[Category: Single protein]]
 [[Category: Sus scrofa]]
-[[Category: Krzywda, S.]]
+[[Category: Krzywda S]]
-[[Category: Wilkinson, A J.]]
+[[Category: Wilkinson AJ]]
-[[Category: oxygen storage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:28 2008''

1mni

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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

Structural highlights

Function

Evolutionary Conservation

See Also

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