1ofj

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(New page: 200px<br /><applet load="1ofj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ofj, resolution 1.80&Aring;" /> '''RECOMBINANT SPERM WH...)
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[[Image:1ofj.jpg|left|200px]]<br /><applet load="1ofj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ofj, resolution 1.80&Aring;" />
 
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'''RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)'''<br />
 
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==Overview==
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==RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)==
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To clarify how the location of distal histidine affects the activation, process of H2O2 by heme proteins, we have characterized reactions with, H2O2 for the L29H/H64L and F43H/H64L mutants of sperm whale myoglobin, (Mb), designed to locate the histidine farther from the heme iron. Whereas, the L29H/H64L double substitution retarded the reaction with H2O2, an, 11-fold rate increase versus wild-type Mb was observed for the F43H/H64L, mutant. The Vmax values for 1-electron oxidations by the myoglobins, correlate well with the varied reactivities with H2O2. The functions of, the distal histidine as a general acid-base catalyst were examined based, on the reactions with cumene hydroperoxide and cyanide, and only the, histidine in F43H/H64L Mb was suggested to facilitate heterolysis of the, peroxide bond. The x-ray crystal structures of the mutants confirmed that, the distal histidines in F43H/H64L Mb and peroxidase are similar in, distance from the heme iron, whereas the distal histidine in L29H/H64L Mb, is located too far to enhance heterolysis. Our results indicate that the, proper positioning of the distal histidine is essential for the activation, of H2O2 by heme enzymes.
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<StructureSection load='1ofj' size='340' side='right'caption='[[1ofj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ofj]] 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=1OFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OFJ 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]] 1.8&#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=1ofj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ofj OCA], [https://pdbe.org/1ofj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ofj RCSB], [https://www.ebi.ac.uk/pdbsum/1ofj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ofj 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/of/1ofj_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=1ofj 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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1OFJ 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 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=1OFJ 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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Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide., Matsui T, Ozaki S, Liong E, Phillips GN Jr, Watanabe Y, J Biol Chem. 1999 Jan 29;274(5):2838-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9915818 9915818]
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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: Liong EC]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Phillips Jr GN]]
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[[Category: Liong, E.C.]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: heme]]
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[[Category: muscle protein]]
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[[Category: oxygen transport]]
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[[Category: peroxidase activity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:56:37 2007''
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Current revision

RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)

PDB ID 1ofj

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