2oif

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{{Seed}}
 
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[[Image:2oif.png|left|200px]]
 
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==The crystal structure of ferric cyanide bound barley hexacoordinate hemoglobin.==
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The line below this paragraph, containing "STRUCTURE_2oif", creates the "Structure Box" on the page.
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<StructureSection load='2oif' size='340' side='right'caption='[[2oif]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[2oif]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OIF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#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=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr>
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{{STRUCTURE_2oif| PDB=2oif | 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=2oif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oif OCA], [https://pdbe.org/2oif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oif RCSB], [https://www.ebi.ac.uk/pdbsum/2oif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oif ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HBL_HORVU HBL_HORVU] May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule.
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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/oi/2oif_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=2oif 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 evolution of oxygen transport hemoglobins occurred on at least two independent occasions. The earliest event led to myoglobin and red blood cell hemoglobin in animals. In plants, oxygen transport "leghemoglobins" evolved much more recently. In both events, pentacoordinate heme sites capable of inert oxygen transfer evolved from hexacoordinate hemoglobins that have unrelated functions. High sequence homology between hexacoordinate and pentacoordinate hemoglobins in plants has poised them for potential structural analysis leading to a molecular understanding of this important evolutionary event. However, the lack of a plant hexacoordinate hemoglobin structure in the exogenously ligand-bound form has prevented such comparison. Here we report the crystal structure of the cyanide-bound hexacoordinate hemoglobin from barley. This presents the first opportunity to examine conformational changes in plant hexacoordinate hemoglobins upon exogenous ligand binding, and reveals structural mechanisms for stabilizing the high-energy pentacoordinate heme conformation critical to the evolution of reversible oxygen binding hemoglobins.
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===The crystal structure of ferric cyanide bound barley hexacoordinate hemoglobin.===
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Plant hemoglobins: a molecular fossil record for the evolution of oxygen transport.,Hoy JA, Robinson H, Trent JT 3rd, Kakar S, Smagghe BJ, Hargrove MS J Mol Biol. 2007 Aug 3;371(1):168-79. Epub 2007 May 18. PMID:17560601<ref>PMID:17560601</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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</div>
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<div class="pdbe-citations 2oif" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17560601}}, adds the Publication Abstract to the page
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17560601 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17560601}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2OIF is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIF OCA].
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==Reference==
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<ref group="xtra">PMID:17560601</ref><references group="xtra"/>
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Hoy, J A.]]
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[[Category: Large Structures]]
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[[Category: Barley]]
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[[Category: Hoy JA]]
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[[Category: Conformational change]]
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[[Category: Evolution]]
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[[Category: Hexacoordinate hemoglobin]]
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[[Category: Ligand binding]]
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[[Category: Non-symbiotic]]
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[[Category: Oxygen transport]]
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[[Category: Symbiotic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:57:51 2009''
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Current revision

The crystal structure of ferric cyanide bound barley hexacoordinate hemoglobin.

PDB ID 2oif

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