3vre: Difference between revisions
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The | ==The crystal structure of hemoglobin from woolly mammoth in the deoxy form== | ||
<StructureSection load='3vre' size='340' side='right'caption='[[3vre]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vre]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammuthus_primigenius Mammuthus primigenius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VRE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vre OCA], [https://pdbe.org/3vre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vre RCSB], [https://www.ebi.ac.uk/pdbsum/3vre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vre ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D3U1H8_MAMPR D3U1H8_MAMPR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The haemoglobin (Hb) of the extinct woolly mammoth has been recreated using recombinant genes expressed in Escherichia coli. The globin gene sequences were previously determined using DNA recovered from frozen cadavers. Although highly similar to the Hb of existing elephants, the woolly mammoth protein shows rather different responses to chloride ions and temperature. In particular, the heat of oxygenation is found to be much lower in mammoth Hb, which appears to be an adaptation to the harsh high-latitude climates of the Pleistocene Ice Ages and has been linked to heightened sensitivity of the mammoth protein to protons, chloride ions and organic phosphates relative to that of Asian elephants. To elucidate the structural basis for the altered homotropic and heterotropic effects, the crystal structures of mammoth Hb have been determined in the deoxy, carbonmonoxy and aquo-met forms. These models, which are the first structures of Hb from an extinct species, show many features reminiscent of human Hb, but underline how the delicate control of oxygen affinity relies on much more than simple overall quaternary-structure changes. | |||
Structures of haemoglobin from woolly mammoth in liganded and unliganded states.,Noguchi H, Campbell KL, Ho C, Unzai S, Park SY, Tame JR Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1441-9. doi:, 10.1107/S0907444912029459. Epub 2012 Oct 18. PMID:23090393<ref>PMID:23090393</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vre" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mammuthus primigenius]] | |||
[[Category: Campbell KL]] | |||
[[Category: Ho C]] | |||
[[Category: Noguchi H]] | |||
[[Category: Park S-Y]] | |||
[[Category: Tame JRH]] | |||
