5ych: Difference between revisions
New page: '''Unreleased structure''' The entry 5ych is ON HOLD until Paper Publication Authors: Isogai, Y., Imamura, H., Nakae, S., Sumi, T., Takahashi, K., Nakagawa, T., Tsuneshige, A., Shirai, ... |
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==Ancestral myoglobin aMbWb of Basilosaurus relative (monophyly)== | |||
<StructureSection load='5ych' size='340' side='right'caption='[[5ych]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ych]] 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=5YCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCH 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]] 1.354Å</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>, <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=5ych FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ych OCA], [https://pdbe.org/5ych PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ych RCSB], [https://www.ebi.ac.uk/pdbsum/5ych PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ych ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MYG_BALMY MYG_BALMY] 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> | |||
[[Category: | </div> | ||
[[Category: Imamura | <div class="pdbe-citations 5ych" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Nakagawa | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Sumi | <references/> | ||
[[Category: Takahashi | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Physeter catodon]] | |||
[[Category: Imamura H]] | |||
[[Category: Isogai Y]] | |||
[[Category: Nakae S]] | |||
[[Category: Nakagawa T]] | |||
[[Category: Shirai T]] | |||
[[Category: Sumi T]] | |||
[[Category: Takahashi K]] | |||
[[Category: Tsuneshige A]] | |||