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1mob

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(New page: 200px<br /><applet load="1mob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mob, resolution 2.2&Aring;" /> '''HIGH-RESOLUTION CRYST...)
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[[Image:1mob.gif|left|200px]]<br /><applet load="1mob" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mob, resolution 2.2&Aring;" />
 
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'''HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN'''<br />
 
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==Overview==
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==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==
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The highly conserved distal histidine residue (His64) of sperm whale, myoglobin modulates the affinity of ligands. In an effort to fully, characterize the effects of mutating residue 64, we have determined the, high-resolution crystal structures of the Gly64, Val64, Leu64, Thr64 and, Gln64 mutants in several liganded forms. Metmyoglobins with hydrophobic, substitutions at residue 64 (Val64 and Leu64) lack a water molecule at the, sixth coordination position, while those with polar amino acid residues at, this position (wild-type and Gln64) retain a covalently bound water, molecule. In the Thr64 mutant, the bound water position is only partially, occupied. In contrast, mutating the distal histidine residue to glycine, does not cause loss of the coordinated water molecule, because the, hydrogen bond from the imidazole side-chain is replaced by one from a, well-ordered solvent water molecule. Differences in water structure around, the distal pocket are apparent also in the structures of deoxymyoglobin, mutants. The water molecule that is hydrogen-bonded to the N epsilon atom, of histidine 64 in wild-type deoxymyoglobin is not found in any of the, position 64 mutant structures that were determined. Comparison of the, carbonmonoxy structures of wild-type, Gly64, Leu64 and Gln64 myoglobins in, the P6 crystal form shows that the conformation of the Fe-C-O complex is, nearly linear and is independent of the identity of the amino acid residue, at position 64. However, the effect of CO binding on the conformation of, residue 64 is striking. Superposition of deoxy and carbonmonoxy structures, reveals significant displacements of the residue 64 side-chain in the, wild-type and Gln64 myoglobins, but no displacement in the Leu64 mutant., These detailed structural studies provide key insights into the mechanisms, of ligand binding and discrimination in myoglobin.
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<StructureSection load='1mob' size='340' side='right'caption='[[1mob]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mob]] 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=1MOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOB 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]] 2.2&#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=1mob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mob OCA], [https://pdbe.org/1mob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mob RCSB], [https://www.ebi.ac.uk/pdbsum/1mob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mob 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/mo/1mob_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=1mob 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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1MOB 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=1MOB 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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High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin., Quillin ML, Arduini RM, Olson JS, Phillips GN Jr, J Mol Biol. 1993 Nov 5;234(1):140-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8230194 8230194]
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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: Phillips Jr GN]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Quillin ML]]
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[[Category: Quillin, M.L.]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: oxygen storage]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:34:52 2007''
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Current revision

HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN

PDB ID 1mob

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