5ycg

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==Ancestral myoglobin aMbWp of Pakicetus relative==
==Ancestral myoglobin aMbWp of Pakicetus relative==
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<StructureSection load='5ycg' size='340' side='right' caption='[[5ycg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5ycg' size='340' side='right'caption='[[5ycg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ycg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YCG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ycg]] 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=5YCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCG FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5yce|5yce]]</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<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=5ycg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycg OCA], [http://pdbe.org/5ycg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ycg RCSB], [http://www.ebi.ac.uk/pdbsum/5ycg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycg ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ycg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycg OCA], [https://pdbe.org/5ycg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ycg RCSB], [https://www.ebi.ac.uk/pdbsum/5ycg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycg ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ycg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Imamura, H]]
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[[Category: Large Structures]]
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[[Category: Isogai, Y]]
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[[Category: Physeter catodon]]
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[[Category: Nakae, S]]
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[[Category: Imamura H]]
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[[Category: Nakagawa, T]]
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[[Category: Isogai Y]]
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[[Category: Shirai, T]]
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[[Category: Nakae S]]
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[[Category: Sumi, T]]
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[[Category: Nakagawa T]]
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[[Category: Takahashi, K]]
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[[Category: Shirai T]]
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[[Category: Tsuneshige, A]]
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[[Category: Sumi T]]
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[[Category: Ancient protein]]
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[[Category: Takahashi K]]
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[[Category: Deep-sea adaptation]]
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[[Category: Tsuneshige A]]
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[[Category: Globin]]
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[[Category: Molecular archaeology]]
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[[Category: Oxygen storage]]
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[[Category: Protein evolution]]
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Ancestral myoglobin aMbWp of Pakicetus relative

PDB ID 5ycg

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