1rse

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(New page: 200px<br /><applet load="1rse" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rse, resolution 1.7&Aring;" /> '''MYOGLOBIN (HORSE HEAR...)
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[[Image:1rse.gif|left|200px]]<br /><applet load="1rse" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rse, resolution 1.7&Aring;" />
 
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'''MYOGLOBIN (HORSE HEART) MUTANT WITH SER 92 REPLACED BY ASP (S92D)'''<br />
 
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==Overview==
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==MYOGLOBIN (HORSE HEART) MUTANT WITH SER 92 REPLACED BY ASP (S92D)==
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The structural and functional consequences of the introduction of a, negatively charged amino acid into the active site of horse heart, myoglobin have been investigated by replacement of the proximal Ser92, residue (F7) with an aspartyl residue (Ser92Asp). UV-visible absorption, maxima of various ferrous and ferric derivatives and low-temperature EPR, spectra of the metaquo (metMb) derivative indicate that the active site, coordination geometry has not been perturbed significantly in the variant., 1H-NMR spectroscopy provides direct evidence for the existence of a distal, water molecule as the sixth ligand in the oxidized form of the variant at, pD 5.7. Spectrophotometric pH titration of the Ser92Asp variant is, consistent with this finding and with a pKa = 8.90 +/- 0.02 [25.0 degrees, C, mu = 0.10 M (NaCl)] for titration of the distal water molecule, identical to the value reported for the wild-type protein. X-ray, crystallography of the metMb derivative indicates that the heme, substituents conserve their orientations in the variant protein, except, for a slight reorientation of the pyrrole A propionate group to which, Ser92 normally hydrogen bonds and reorientation of the carboxyl end of the, pyrrole D propionate group. No change is observed in conformation of the, proximal (His93) or distal (Wat156) heme ligands. 1H-NMR spectroscopy of, the metMbCN form of the protein indicates that a slight rotation of the, proximal His93 ligand has occurred in this derivative. Resonance Raman, experiments indicate increased conformational heterogeneity in the, proximal pocket of the variant. Failure to detect electron density for the, Asp residue in the X-ray diffraction map of the variant protein and high, average thermal factors for the pyrrole A propionate substituent are, consistent with this observation. The variant exhibits novel pH-dependent, behavior in the metMb form, as shown by 1H-NMR spectroscopy, and provides, evidence for a heme-linked titratable group with a pKa of 5.4 in this, derivative. The metMbCN and deoxyMb derivatives also exhibit pH-dependent, behavior, with pKas of 5.60 +/- 0.07 and 6.60 +/- 0.07, respectively, compared to the wild-type values of 5.4 +/- 0.04 and 5.8 +/- 0.1. The, heme-linked ionizable group is proposed to be His97 in all three, derivatives. The reduction potential of the variant is 72 +/- 2 mV vs SHE, [25.0 degrees C, mu = 0.10 M (phosphate), pH 6.0], an increase of 8 mV, over the wild-type value. The possible influence of a number of variables, on the magnitude of the reduction potential in myoglobin and other heme, proteins is discussed.
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<StructureSection load='1rse' size='340' side='right'caption='[[1rse]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rse]] 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=1RSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSE 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=1rse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rse OCA], [https://pdbe.org/1rse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rse RCSB], [https://www.ebi.ac.uk/pdbsum/1rse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rse 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/rs/1rse_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=1rse 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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1RSE 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=1RSE 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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Electrostatic modification of the active site of myoglobin: characterization of the proximal Ser92Asp variant., Lloyd E, Burk DL, Ferrer JC, Maurus R, Doran J, Carey PR, Brayer GD, Mauk AG, Biochemistry. 1996 Sep 10;35(36):11901-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8794773 8794773]
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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: Burk, D.L.]]
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[[Category: Burk DL]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: heme]]
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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 01:50:21 2007''
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Current revision

MYOGLOBIN (HORSE HEART) MUTANT WITH SER 92 REPLACED BY ASP (S92D)

PDB ID 1rse

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