1yoi

<StructureSection load='1yoi' size='340' side='right' caption='[[1yoi]], [[Resolution|resolution]] 1.65&Aring;' scene=''>

<table><tr><td colspan='2'>[[1yoi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YOI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COH:PROTOPORPHYRIN+IX+CONTAINING+CO'>COH</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yoi OCA], [http://pdbe.org/1yoi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yoi RCSB], [http://www.ebi.ac.uk/pdbsum/1yoi PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yo/1yoi_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The structures of the deoxy, oxy, and aquomet forms of native sperm whale myoglobin reconstituted with cobalt protoporphyrin IX have been determined by x-ray crystallography. As expected, cobalt myoglobin closely resembles native iron myoglobin in overall structure, especially in their respective aquomet forms. In the cobalt oxymyoglobin structure, the Nepsilon of distal histidine 64 lies within hydrogen bonding distance to both the oxygen atom directly bonded to the cobalt and the terminal oxygen atom, in agreement with previous EPR and resonance Raman studies. The metal atom in cobaltous myoglobin does show a small 0.06-A out-of-porphyrin plane displacement when moving from the oxy to deoxy state. In the case of the native iron-containing myoglobin, the oxy to deoxy transition results in a larger 0.16-A displacement of the metal farther out of the porphyrin plane, attributed to an increase in spin from S = 0 to S = 2. The small displacement in cobalt myoglobin is due to a change in coordination geometry, not spin state (S = 1/2 for both cobalt deoxy- and oxymyoglobin). The small out-of-porphyrin plane movement of cobalt which accompanies deoxygenation of myoglobin also occurs in cobalt hemoglobin and serves to explain why cooperativity, although reduced, is still preserved when iron is replaced by cobalt in human hemoglobin.

High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin.,Brucker EA, Olson JS, Phillips GN Jr, Dou Y, Ikeda-Saito M J Biol Chem. 1996 Oct 11;271(41):25419-22. PMID:8810310<ref>PMID:8810310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Myoglobin|Myoglobin]]

[[Category: Brucker, E A]]

[[Category: Phillips, G N]]

[[Category: Respiratory protein]]