1tes

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(New page: 200px<br /> <applet load="1tes" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tes, resolution 1.7&Aring;" /> '''OXYGEN BINDING MUSCL...)
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[[Image:1tes.gif|left|200px]]<br />
 
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<applet load="1tes" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tes, resolution 1.7&Aring;" />
 
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'''OXYGEN BINDING MUSCLE PROTEIN'''<br />
 
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==Overview==
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==OXYGEN BINDING MUSCLE PROTEIN==
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Nitric oxide (NO) has been implicated as mediator in a variety of, physiological functions, including neurotransmission, platelet, aggregation, macrophage function, and vasodilation. The consumption of NO, by extracellular hemoglobin and subsequent vasoconstriction have been, suggested to be the cause of the mild hypertensive events reported during, in vivo trials of hemoglobin-based O2 carriers. The depletion of NO from, endothelial cells is most likely due to the oxidative reaction of NO with, oxyhemoglobin in arterioles and surrounding tissue. In order to determine, the mechanism of this key reaction, we have measured the kinetics of, NO-induced oxidation of a variety of different recombinant sperm whale, myoglobins (Mb) and human hemoglobins (Hb). The observed rates depend, linearly on [NO] but show no dependence on [O2]. The bimolecular rate, constants for NO-induced oxidation of MbO2 and HbO2 are large (k.ox,NO =, 30-50 microM-1 s-1 for the wild-type proteins) and similar to those for, simple nitric oxide binding to deoxygenated Mb and Hb. Both reversible NO, binding and NO-induced oxidation occur in two steps: (1) bimolecular entry, of nitric oxide into the distal portion of the heme pocket and (2) rapid, reaction of noncovalently bound nitric oxide with the iron atom to produce, Fe(2+)-N=O or with Fe(2+)-O-O delta- to produce Fe(3+)-OH2 and nitrate., Both the oxidation and binding rate constants for sperm whale Mb were, increased when His(E7) was replaced by aliphatic residues. These mutants, lack polar interactions in the distal pocket which normally hinder NO, entry into the protein. Decreasing the volume of the distal pocket by, replacing Leu(B10) and Val(E11) with aromatic amino acids markedly, inhibits NO-induced oxidation of MbO2. The latter results provide a, protein engineering strategy for reducing hypertensive events caused by, extracellular hemoglobin-based O2 carriers. This approach has been, explored by examining the effects of Phe(B10) and Phe(E11) substitutions, on the rates of NO-induced oxidation of the alpha and beta subunits in, recombinant human hemoglobin.
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<StructureSection load='1tes' size='340' side='right'caption='[[1tes]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tes]] 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=1TES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TES 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=ETN:METHYLETHYLAMINE'>ETN</scene>, <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=1tes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tes OCA], [https://pdbe.org/1tes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tes RCSB], [https://www.ebi.ac.uk/pdbsum/1tes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tes 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/te/1tes_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=1tes 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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1TES 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, HEM and ETN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TES 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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Mechanism of NO-induced oxidation of myoglobin and hemoglobin., Eich RF, Li T, Lemon DD, Doherty DH, Curry SR, Aitken JF, Mathews AJ, Johnson KA, Smith RD, Phillips GN Jr, Olson JS, Biochemistry. 1996 Jun 4;35(22):6976-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8679521 8679521]
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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: Olson JS]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Phillips Jr GN]]
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[[Category: Olson, J.S.]]
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[[Category: Smith RD]]
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[[Category: Smith, R.D.]]
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[[Category: ETN]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: myoglobin (ethyl isocyanide)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:18:48 2007''
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Current revision

OXYGEN BINDING MUSCLE PROTEIN

PDB ID 1tes

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