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[[Image: | ==CARBONMONOXY TROUT HEMOGLOBIN I== | ||
<StructureSection load='1ouu' size='340' side='right' caption='[[1ouu]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ouu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OUU FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ouu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ouu RCSB], [http://www.ebi.ac.uk/pdbsum/1ouu PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ouu_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. | |||
The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.,Tame JR, Wilson JC, Weber RE J Mol Biol. 1996 Jun 21;259(4):749-60. PMID:8683580<ref>PMID:8683580</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hemoglobin|Hemoglobin]] | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Oncorhynchus mykiss]] | [[Category: Oncorhynchus mykiss]] | ||
[[Category: Tame, J.]] | [[Category: Tame, J.]] | ||
Revision as of 02:28, 29 September 2014
CARBONMONOXY TROUT HEMOGLOBIN ICARBONMONOXY TROUT HEMOGLOBIN I
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.,Tame JR, Wilson JC, Weber RE J Mol Biol. 1996 Jun 21;259(4):749-60. PMID:8683580[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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