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1obm

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(New page: 200px<br /> <applet load="1obm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obm, resolution 1.85&Aring;" /> '''RECOMBINANT SPERM W...)
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[[Image:1obm.gif|left|200px]]<br />
 
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<applet load="1obm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1obm, resolution 1.85&Aring;" />
 
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'''RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)'''<br />
 
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==Overview==
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==RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)==
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The bivalve mollusc Lucina pectinata harbors sulfide-oxidizing, chemoautotrophic bacteria and expresses a monomeric hemoglobin I, HbI, with normal O2, but extraordinarily high sulfide affinity. The crystal, structure of aquomet Lucina HbI has revealed an active site with three, residues not commonly found in vertebrate globins: Phe(B10), Gln(E7), and, Phe(E11) (Rizzi, M., Wittenberg, J. B., Coda, A., Fasano, M., Ascenzi, P., and Bolognesi, M. (1994) J. Mol. Biol. 244, 86-89). Engineering these, three residues into sperm whale myoglobin results in a triple mutant with, approximately 700-fold higher sulfide affinity than for wild-type. The, single crystal x-ray structure of the aquomet derivative of the myoglobin, triple mutant and the solution 1H NMR active site structures of the, cyanomet derivatives of both the myoglobin mutant and Lucina HbI have been, determined to examine further the structural origin of their unusually, high sulfide affinities. The major differences in the distal pocket is, that in the aquomet form the carbonyl of Gln64(E7) serves as a H-bond, acceptor, whereas in the cyanomet form the amido group acts as H-bond, donor to the bound ligand. Phe68(E11) is rotated approximately 90 degrees, about chi2 and located approximately 1-2 A closer to the iron atom in the, myoglobin triple mutant relative to its conformation in Lucina HbI. The, change in orientation potentially eliminates the stabilizing interaction, with sulfide and, together with the decrease in size of the distal pocket, accounts for the 7-fold lower sulfide affinity of the myoglobin mutant, compared with that of Lucina HbI.
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<StructureSection load='1obm' size='340' side='right'caption='[[1obm]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1obm]] 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=1OBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OBM 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]] 1.85&#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=1obm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obm OCA], [https://pdbe.org/1obm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1obm RCSB], [https://www.ebi.ac.uk/pdbsum/1obm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1obm 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/ob/1obm_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=1obm 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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1OBM 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=1OBM 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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Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata., Nguyen BD, Zhao X, Vyas K, La Mar GN, Lile RA, Brucker EA, Phillips GN Jr, Olson JS, Wittenberg JB, J Biol Chem. 1998 Apr 17;273(16):9517-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9545280 9545280]
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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: Brucker EA]]
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[[Category: Brucker, E.A.]]
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[[Category: Lile RA]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Phillips Jr GN]]
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[[Category: Lile, R.A.]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: oxygen binding muscle protein]]
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[[Category: oxygen transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:15:24 2007''
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Current revision

RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)

PDB ID 1obm

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