1mwc

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(New page: 200px<br /><applet load="1mwc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwc, resolution 1.7&Aring;" /> '''WILD TYPE MYOGLOBIN W...)
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[[Image:1mwc.jpg|left|200px]]<br /><applet load="1mwc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mwc, resolution 1.7&Aring;" />
 
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'''WILD TYPE MYOGLOBIN WITH CO'''<br />
 
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==Overview==
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==WILD TYPE MYOGLOBIN WITH CO==
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The isopropyl side chain of valine68 in myoglobin has been replaced by the, acetamide side chain of asparagine in an attempt to engineer higher oxygen, affinity. The asparagine replacement introduces a second hydrogen bond, donor group into the distal heme pocket which could further stabilize, bound oxygen. The Val68 to Asn substitution leads to approximately 3-fold, increases in oxygen affinity and 4-6-fold decreases in CO affinity. As a, result, the M-value (KCO/KO2) is lowered 15-20-fold to a value close to, unity. An even larger enhancement of O2 affinity is seen when asparagine68, is inserted into H64L sperm whale myoglobin which lacks a distal, histidine. The overall rate constants for oxygen and carbon monoxide, binding to the single V68N myoglobin mutants are uniformly lower than, those for the wild-type protein. In contrast, the overall rate constant, for NO association is unchanged. Analyses of time courses monitoring the, geminate recombination of ligands following nanosecond and picosecond, flash photolysis of MbNO and MbO2 indicate that the barrier to ligand, binding from within the heme pocket has been raised with little effect on, the barrier to diffusion of the ligand into the pocket from the solvent., The crystal structures of the aquomet, deoxy, oxy, and carbon monoxy forms, of the V68N mutant have been determined to resolutions ranging from 1.75, to 2.2 A at 150 K. The overall structures are very similar to those of the, wild-type protein with the principal alterations taking place within and, around the distal heme pocket. In all four structures the asparagine68, side chain lies almost parallel to the plane of the heme with its amide, group directed toward the back of the distal heme pocket. The coordinated, water molecule in the aquomet form and the bound oxygen in the oxy form, can form hydrogen-bonding interactions with both the Asn68 amide group and, the imidazole side chain of His64. Surprisingly, in the carbon monoxy form, of the V68N mutant, the histidine64 side chain has swung completely out, the distal pocket, its place being taken by two ordered water molecules., Overall, these functional and structural results show that the, asparagine68 side chain (i) forms a strong hydrogen bond with bound oxygen, through its -NH2 group but (ii) sterically hinders the approach of ligands, to the iron from within the distal heme pocket.
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<StructureSection load='1mwc' size='340' side='right'caption='[[1mwc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mwc]] 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=1MWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWC 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]] 1.7&#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></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=1mwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwc OCA], [https://pdbe.org/1mwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwc RCSB], [https://www.ebi.ac.uk/pdbsum/1mwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwc 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/mw/1mwc_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=1mwc 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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1MWC 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 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=1MWC 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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Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution., Krzywda S, Murshudov GN, Brzozowski AM, Jaskolski M, Scott EE, Klizas SA, Gibson QH, Olson JS, Wilkinson AJ, Biochemistry. 1998 Nov 10;37(45):15896-907. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9843395 9843395]
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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: Brzozowski, A.M.]]
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[[Category: Brzozowski AM]]
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[[Category: Gibson, Q.H.]]
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[[Category: Gibson QH]]
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[[Category: Jaskolski, M.]]
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[[Category: Jaskolski M]]
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[[Category: Klizas, S.A.]]
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[[Category: Klizas SA]]
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[[Category: Krzywda, S.]]
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[[Category: Krzywda S]]
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[[Category: Murshudov, G.N.]]
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[[Category: Murshudov GN]]
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[[Category: Olson, J.S.]]
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[[Category: Olson JS]]
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[[Category: Scott, E.E.]]
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[[Category: Scott EE]]
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[[Category: Wilkinson, A.J.]]
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[[Category: Wilkinson AJ]]
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[[Category: CMO]]
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[[Category: HEM]]
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[[Category: co]]
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[[Category: myoglobin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:45:37 2007''
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Current revision

WILD TYPE MYOGLOBIN WITH CO

PDB ID 1mwc

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