1f5p: Difference between revisions

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{{Seed}}
[[Image:1f5p.png|left|200px]]


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==2.9 ANGSTROM CRYSTAL STRUCTURE OF LAMPREY HEMOGLOBIN THAT HAS BEEN EXPOSED TO CARBON MONOXIDE.==
The line below this paragraph, containing "STRUCTURE_1f5p", creates the "Structure Box" on the page.
<StructureSection load='1f5p' size='340' side='right'caption='[[1f5p]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1f5p]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Petromyzon_marinus Petromyzon marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5P FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#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=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
{{STRUCTURE_1f5p|  PDB=1f5p  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5p OCA], [https://pdbe.org/1f5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5p RCSB], [https://www.ebi.ac.uk/pdbsum/1f5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB5_PETMA GLB5_PETMA]
== 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/f5/1f5p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1f5p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hemoglobins of the Sea Lamprey (Petromyzon marinus) exist in an equilibrium between low affinity oligomers, stabilized by proton binding, and higher affinity monomers, stabilized by oxygen binding. Recent crystallographic analysis revealed that dimerization is coupled with key changes at the ligand binding site with the distal histidine sterically restricting ligand binding in the deoxy dimer but with no significant structural rearrangements on the proximal side. These structural insights led to the hypothesis that oxygen affinity of lamprey hemoglobin is distally regulated. Here we present the 2.9-A crystal structure of deoxygenated lamprey hemoglobin in an orthorhombic crystal form along with the structure of these crystals exposed to carbon monoxide. The hexameric assemblage in this crystal form is very similar to those observed in the previous deoxy structure. Whereas the hydrogen bonding network and packing contacts formed in the dimeric interface of lamprey hemoglobin are largely unaffected by ligand binding, the binding of carbon monoxide induces the distal histidine to swing to positions that would preclude the formation of a stabilizing hydrogen bond with the bound ligand. These results suggest a dual role for the distal histidine and strongly support the hypothesis that ligand affinity in lamprey hemoglobin is distally regulated.


===2.9 ANGSTROM CRYSTAL STRUCTURE OF LAMPREY HEMOGLOBIN THAT HAS BEEN EXPOSED TO CARBON MONOXIDE.===
Crystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinity.,Heaslet HA, Royer WE Jr J Biol Chem. 2001 Jul 13;276(28):26230-6. Epub 2001 May 4. PMID:11340069<ref>PMID:11340069</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f5p" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11340069}}, adds the Publication Abstract to the page
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11340069 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11340069}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1F5P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Petromyzon_marinus Petromyzon marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5P OCA].
 
==Reference==
Crystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinity., Heaslet HA, Royer WE Jr, J Biol Chem. 2001 Jul 13;276(28):26230-6. Epub 2001 May 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11340069 11340069]
[[Category: Petromyzon marinus]]
[[Category: Petromyzon marinus]]
[[Category: Single protein]]
[[Category: Heaslet HA]]
[[Category: Heaslet, H A.]]
[[Category: Royer Jr WE]]
[[Category: Jr., W E.Royer.]]
[[Category: Crystalline ligand transition]]
[[Category: Heme]]
[[Category: Hemoglobin]]
[[Category: Lamprey]]
 
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Retrieved from "https://proteopedia.org/1f5p"