1i4z

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[[Image:1i4z.gif|left|200px]]
 
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{{Structure
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==THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII L98Y METHEMERYTHRIN==
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|PDB= 1i4z |SIZE=350|CAPTION= <scene name='initialview01'>1i4z</scene>, resolution 2.10&Aring;
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<StructureSection load='1i4z' size='340' side='right'caption='[[1i4z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>
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<table><tr><td colspan='2'>[[1i4z]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Phascolopsis_gouldii Phascolopsis gouldii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I4Z FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
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|DOMAIN=
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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=1i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4z OCA], [https://pdbe.org/1i4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i4z RCSB], [https://www.ebi.ac.uk/pdbsum/1i4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4z ProSAT]</span></td></tr>
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|RELATEDENTRY=[[999|999]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4z OCA], [http://www.ebi.ac.uk/pdbsum/1i4z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i4z RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HEMT_PHAGO HEMT_PHAGO] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
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== Evolutionary Conservation ==
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'''THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII L98Y METHEMERYTHRIN'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/1i4z_consurf.spt"</scriptWhenChecked>
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Reported are the X-ray crystal structures of recombinant Phascolopsis gouldii methemerythrin (1.8-A resolution) and the structure of an O2-binding-pocket mutant, L98Y methemerythrin (2.1-A resolution). The L98Y hemerythrin (Hr) has a greatly enhanced O2 affinity, a slower O2 dissociation rate, a larger solvent deuterium isotope effect on this rate, and a greater resistance to autoxidation relative to the wild-type protein. The crystal structures show that the hydrophobic binding pocket of Hr can accommodate substitution of a leucyl by a tyrosyl side chain with relatively minor structural rearrangements. UV/vis and resonance Raman spectra show that in solution L98Y methemerythrin contains a mixture of two diiron site structures differing by the absence or presence of an Fe(III)-coordinated phenolate. However, in the crystal, only one L98Y diiron site structure is seen, in which the Y98 hydroxyl is not a ligand, but instead forms a hydrogen bond to a terminal hydroxo/aqua ligand to the nearest iron. Based on this crystal structure, we propose that in the oxy form of L98Y hemerythrin the non-polar nature of the binding pocket favors localization of the Y98 hydroxyl near the O2 binding site, where it can donate a hydrogen bond to the hydroperoxo ligand. The stabilizing Y98OH-O2H-interaction would account for all of the altered O2 binding properties of L98Y Hr listed above.
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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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==About this Structure==
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</jmolCheckbox>
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1I4Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phascolopsis_gouldii Phascolopsis gouldii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4Z OCA].
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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=1i4z ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket., Farmer CS, Kurtz DM Jr, Liu ZJ, Wang BC, Rose J, Ai J, Sanders-Loehr J, J Biol Inorg Chem. 2001 Apr;6(4):418-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11372200 11372200]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Phascolopsis gouldii]]
[[Category: Phascolopsis gouldii]]
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[[Category: Single protein]]
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[[Category: Farmer CS]]
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[[Category: Farmer, C S.]]
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[[Category: Kurtz Jr DM]]
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[[Category: Jr., D M.Kurtz.]]
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[[Category: Liu Z-J]]
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[[Category: Liu, Z J.]]
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[[Category: Rose J]]
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[[Category: Rose, J.]]
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[[Category: Wang BC]]
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[[Category: Wang, B C.]]
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[[Category: diiron]]
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[[Category: four-helix bundle]]
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[[Category: hemerythrin]]
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[[Category: mutation]]
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[[Category: oxygen binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:43 2008''
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Current revision

THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII L98Y METHEMERYTHRIN

PDB ID 1i4z

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