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==Ancestral myoglobin aMbWb of Basilosaurus relative (monophyly)==
==Ancestral myoglobin aMbWb of Basilosaurus relative (monophyly)==
<StructureSection load='5ych' size='340' side='right' caption='[[5ych]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='5ych' size='340' side='right'caption='[[5ych]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ych]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YCH FirstGlance]. <br>
<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='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]] 1.354&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5yce|5yce]], [[5ycg|5ycg]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ych FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ych OCA], [http://pdbe.org/5ych PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ych RCSB], [http://www.ebi.ac.uk/pdbsum/5ych PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ych ProSAT]</span></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>
</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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ych" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ych" style="background-color:#fffaf0;"></div>
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Phycd]]
[[Category: Large Structures]]
[[Category: Imamura, H]]
[[Category: Physeter catodon]]
[[Category: Isogai, Y]]
[[Category: Imamura H]]
[[Category: Nakae, S]]
[[Category: Isogai Y]]
[[Category: Nakagawa, T]]
[[Category: Nakae S]]
[[Category: Shirai, T]]
[[Category: Nakagawa T]]
[[Category: Sumi, T]]
[[Category: Shirai T]]
[[Category: Takahashi, K]]
[[Category: Sumi T]]
[[Category: Tsuneshige, A]]
[[Category: Takahashi K]]
[[Category: Ancient protein]]
[[Category: Tsuneshige A]]
[[Category: Deep-sea adaptation]]
[[Category: Globin]]
[[Category: Molecular archaeology]]
[[Category: Oxygen storage]]
[[Category: Protein evolution]]

Latest revision as of 11:26, 22 November 2023

Ancestral myoglobin aMbWb of Basilosaurus relative (monophyly)Ancestral myoglobin aMbWb of Basilosaurus relative (monophyly)

Structural highlights

5ych is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.354Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_BALMY Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Isogai Y, Imamura H, Nakae S, Sumi T, Takahashi KI, Nakagawa T, Tsuneshige A, Shirai T. Tracing whale myoglobin evolution by resurrecting ancient proteins. Sci Rep. 2018 Nov 15;8(1):16883. doi: 10.1038/s41598-018-34984-6. PMID:30442991 doi:http://dx.doi.org/10.1038/s41598-018-34984-6

5ych, resolution 1.35Å

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