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==Sperm whale myoglobin swMb== | ==Sperm whale myoglobin swMb== | ||
<StructureSection load='5yce' size='340' side='right' caption='[[5yce]], [[Resolution|resolution]] 0.77Å' scene=''> | <StructureSection load='5yce' size='340' side='right'caption='[[5yce]], [[Resolution|resolution]] 0.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yce]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5yce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.77Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5yce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yce OCA], [https://pdbe.org/5yce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yce RCSB], [https://www.ebi.ac.uk/pdbsum/5yce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yce ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Extant cetaceans, such as sperm whale, acquired the great ability to dive into the ocean depths during the evolution from their terrestrial ancestor that lived about 50 million years ago. Myoglobin (Mb) is highly concentrated in the myocytes of diving animals, in comparison with those of land animals, and is thought to play a crucial role in their adaptation as the molecular aqualung. Here, we resurrected ancestral whale Mbs, which are from the common ancestor between toothed and baleen whales (Basilosaurus), and from a further common quadrupedal ancestor between whale and hippopotamus (Pakicetus). The experimental and theoretical analyses demonstrated that whale Mb adopted two distinguished strategies to increase the protein concentration in vivo along the evolutionary history of deep sea adaptation; gaining precipitant tolerance in the early phase of the evolution, and increase of folding stability in the late phase. | |||
Tracing whale myoglobin evolution by resurrecting ancient proteins.,Isogai Y, Imamura H, Nakae S, Sumi T, Takahashi KI, Nakagawa T, Tsuneshige A, Shirai T Sci Rep. 2018 Nov 15;8(1):16883. doi: 10.1038/s41598-018-34984-6. PMID:30442991<ref>PMID:30442991</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5yce" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Imamura | [[Category: Large Structures]] | ||
[[Category: Isogai | [[Category: Physeter catodon]] | ||
[[Category: Nakae | [[Category: Imamura H]] | ||
[[Category: Nakagawa | [[Category: Isogai Y]] | ||
[[Category: Shirai | [[Category: Nakae S]] | ||
[[Category: Sumi | [[Category: Nakagawa T]] | ||
[[Category: Takahashi | [[Category: Shirai T]] | ||
[[Category: Tsuneshige | [[Category: Sumi T]] | ||
[[Category: Takahashi K]] | |||
[[Category: Tsuneshige A]] | |||
Latest revision as of 11:26, 22 November 2023
Sperm whale myoglobin swMbSperm whale myoglobin swMb
Structural highlights
FunctionMYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedExtant cetaceans, such as sperm whale, acquired the great ability to dive into the ocean depths during the evolution from their terrestrial ancestor that lived about 50 million years ago. Myoglobin (Mb) is highly concentrated in the myocytes of diving animals, in comparison with those of land animals, and is thought to play a crucial role in their adaptation as the molecular aqualung. Here, we resurrected ancestral whale Mbs, which are from the common ancestor between toothed and baleen whales (Basilosaurus), and from a further common quadrupedal ancestor between whale and hippopotamus (Pakicetus). The experimental and theoretical analyses demonstrated that whale Mb adopted two distinguished strategies to increase the protein concentration in vivo along the evolutionary history of deep sea adaptation; gaining precipitant tolerance in the early phase of the evolution, and increase of folding stability in the late phase. Tracing whale myoglobin evolution by resurrecting ancient proteins.,Isogai Y, Imamura H, Nakae S, Sumi T, Takahashi KI, Nakagawa T, Tsuneshige A, Shirai T Sci Rep. 2018 Nov 15;8(1):16883. doi: 10.1038/s41598-018-34984-6. PMID:30442991[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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