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New page: left|200px<br /><applet load="1ofj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ofj, resolution 1.80Å" /> '''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"
caption="1ofj, resolution 1.80&Aring;" />
'''RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)'''<br />


==Overview==
==RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)==
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.
<StructureSection load='1ofj' size='340' side='right'caption='[[1ofj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] 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/of/1ofj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ofj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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:9915818<ref>PMID:9915818</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 1ofj" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Liong EC]]
[[Category: Jr., G.N.Phillips.]]
[[Category: Phillips Jr GN]]
[[Category: Liong, E.C.]]
[[Category: HEM]]
[[Category: SO4]]
[[Category: heme]]
[[Category: muscle protein]]
[[Category: oxygen transport]]
[[Category: peroxidase activity]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:56:37 2007''

Latest revision as of 06:50, 13 August 2026

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

1ofj, resolution 1.80Å

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