1hmo

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{{Seed}}
 
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[[Image:1hmo.png|left|200px]]
 
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==THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1hmo", creates the "Structure Box" on the page.
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<StructureSection load='1hmo' size='340' side='right'caption='[[1hmo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1hmo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMO 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&#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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
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{{STRUCTURE_1hmo| PDB=1hmo | SCENE= }}
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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=1hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmo OCA], [https://pdbe.org/1hmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmo RCSB], [https://www.ebi.ac.uk/pdbsum/1hmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY] 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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[[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/hm/1hmo_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=1hmo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. Restrained least-squares refinement has produced molecular models giving R-values of 16.8% for deoxy (41,064 reflections from 10 A to 2.0 A) and 17.3% for oxy hemerythrin (40,413 reflections from 10.0 A to 2.0 A). The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. The binuclear complex in each derivative retains an oxygen atom bridging the two iron atoms, but the bond lengths found in deoxy hemerythrin support the idea that, in that form, the bridge is protonated, i.e. the bridging group is a hydroxyl. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom.
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===THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION===
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Structures of deoxy and oxy hemerythrin at 2.0 A resolution.,Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:2016748<ref>PMID:2016748</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_2016748}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1hmo" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 2016748 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_2016748}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1HMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMO OCA].
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==Reference==
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Structures of deoxy and oxy hemerythrin at 2.0 A resolution., Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE, J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2016748 2016748]
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[[Category: Single protein]]
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[[Category: Themiste dyscritum]]
[[Category: Themiste dyscritum]]
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[[Category: Holmes, M A.]]
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[[Category: Holmes MA]]
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[[Category: Letrong, I.]]
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[[Category: Letrong I]]
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[[Category: Sieker, L C.]]
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[[Category: Sieker LC]]
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[[Category: Stenkamp, R E.]]
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[[Category: Stenkamp RE]]
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[[Category: Turley, S.]]
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[[Category: Turley S]]
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[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:24:19 2008''
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Current revision

THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION

PDB ID 1hmo

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