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1wla

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(New page: 200px<br /><applet load="1wla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wla, resolution 1.7&Aring;" /> '''MYOGLOBIN (HORSE HEAR...)
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[[Image:1wla.gif|left|200px]]<br /><applet load="1wla" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wla, resolution 1.7&Aring;" />
 
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'''MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE'''<br />
 
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==Overview==
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==MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE==
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Well-ordered internal amino acids can contribute significantly to the, stability of proteins. To investigate the importance of the hydrophobic, packing interface between helices G and H in the proximal heme pocket of, horse heart myoglobin, the highly conserved amino acid, Leu104, was, substituted with asparagine, a polar amino acid of similar size. The, Leu104Asn mutant protein and its recombinant wild-type horse heart, myoglobin counterpart were expressed from synthetic genes in Escherichia, coli. Thermal denaturation of these two recombinant myoglobins, as studied, by measurement of circular dichroism ellipticity at 222 nm, revealed that, the Leu104Asn mutant had a significantly lower t(m) (71.8 +/- 1 degree C, pH 7.0) than recombinant wild-type myoglobin (81.3 +/- 1 degree C, pH, 7.0). To examine the extent to which this 10 degrees C decrease in thermal, stability was associated with structural perturbations, X-ray diffraction, techniques were used to determine the three-dimensional structures of both, the recombinant wild-type and Leu104Asn myoglobins to 0.17 nm resolution., Refinement of these structures gave final crystallographic R-factors of, 16.0% and 17.9%, respectively. Structural comparison of the natural and, recombinant wild-type myoglobins, together with absorption spectroscopic, and electron paramagnetic resonance (EPR) analyses, confirmed the proper, expression and folding of the recombinant protein in E. coli., Surprisingly, despite the decreased thermal stability of the Leu104Asn, mutant, there are no significant structural differences between the mutant, and wild-type myoglobins. EPR and absorption spectroscopic analyses, further confirmed the similar nature of the heme iron centres in both, proteins. Thus, the introduction of an energetically unfavourable change, in side chain polarity at position 104 into a hydrophobic environment that, does not support the hydrogen bonding potential of the mutant asparagine, appears to perturb important stabilizing helix-helix and heme-protein, interactions. The induced structural destabilization is thereby reflected, by a significant decrease in the t(m) of horse heart myoglobin.
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<StructureSection load='1wla' size='340' side='right'caption='[[1wla]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wla]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLA 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=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=1wla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wla OCA], [https://pdbe.org/1wla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wla RCSB], [https://www.ebi.ac.uk/pdbsum/1wla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wla ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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/wl/1wla_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=1wla 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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1WLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WLA 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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A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket., Maurus R, Overall CM, Bogumil R, Luo Y, Mauk AG, Smith M, Brayer GD, Biochim Biophys Acta. 1997 Aug 15;1341(1):1-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9300804 9300804]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brayer, G.D.]]
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[[Category: Brayer GD]]
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[[Category: Maurus, R.]]
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[[Category: Maurus R]]
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[[Category: HEM]]
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[[Category: SO4]]
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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 05:30:18 2007''
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Current revision

MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE

PDB ID 1wla

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