7ddt: Difference between revisions
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==Ancestral myoglobin aMbSe of Enaliarctos relative (imidazol ligand)== | ==Ancestral myoglobin aMbSe of Enaliarctos relative (imidazol ligand)== | ||
<StructureSection load='7ddt' size='340' side='right'caption='[[7ddt]]' scene=''> | <StructureSection load='7ddt' size='340' side='right'caption='[[7ddt]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDT FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ddt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDT FirstGlance]. <br> | ||
</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=7ddt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddt OCA], [https://pdbe.org/7ddt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddt RCSB], [https://www.ebi.ac.uk/pdbsum/7ddt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddt ProSAT]</span></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]] 2.9Å</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=IMD:IMIDAZOLE'>IMD</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=7ddt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddt OCA], [https://pdbe.org/7ddt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddt RCSB], [https://www.ebi.ac.uk/pdbsum/7ddt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Myoglobin (Mb) is highly concentrated in the myocytes of diving mammals such as whales and seals, in comparison with land animals, and its molecular evolution has played a crucial role in their deep-sea adaptation. We previously resurrected ancestral whale Mbs and demonstrated the evolutional strategies for higher solubility under macromolecular crowding conditions. Pinnipeds, such as seals and sea lions, are also expert diving mammals with Mb-rich muscles. In the present study, we resurrected ancestral pinniped Mbs and investigated their biochemical and structural properties. Comparisons between pinniped and whale Mbs revealed the common and distinctive strategies for the deep-sea adaptation. The overall evolution processes, gaining precipitant tolerance and improving thermodynamic stability, were commonly observed. However, the strategies for improving the folding stability differed, and the pinniped Mbs exploited the shielding of hydrophobic surfaces more effectively than the whale Mbs. | |||
Common and unique strategies of myoglobin evolution for deep-sea adaptation of diving mammals.,Isogai Y, Imamura H, Nakae S, Sumi T, Takahashi KI, Shirai T iScience. 2021 Jul 30;24(8):102920. doi: 10.1016/j.isci.2021.102920. eCollection , 2021 Aug 20. PMID:34430810<ref>PMID:34430810</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ddt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synthetic construct]] | |||
[[Category: Imamura H]] | [[Category: Imamura H]] | ||
[[Category: Isogai Y]] | [[Category: Isogai Y]] | ||
Latest revision as of 19:31, 29 November 2023
Ancestral myoglobin aMbSe of Enaliarctos relative (imidazol ligand)Ancestral myoglobin aMbSe of Enaliarctos relative (imidazol ligand)
Structural highlights
Publication Abstract from PubMedMyoglobin (Mb) is highly concentrated in the myocytes of diving mammals such as whales and seals, in comparison with land animals, and its molecular evolution has played a crucial role in their deep-sea adaptation. We previously resurrected ancestral whale Mbs and demonstrated the evolutional strategies for higher solubility under macromolecular crowding conditions. Pinnipeds, such as seals and sea lions, are also expert diving mammals with Mb-rich muscles. In the present study, we resurrected ancestral pinniped Mbs and investigated their biochemical and structural properties. Comparisons between pinniped and whale Mbs revealed the common and distinctive strategies for the deep-sea adaptation. The overall evolution processes, gaining precipitant tolerance and improving thermodynamic stability, were commonly observed. However, the strategies for improving the folding stability differed, and the pinniped Mbs exploited the shielding of hydrophobic surfaces more effectively than the whale Mbs. Common and unique strategies of myoglobin evolution for deep-sea adaptation of diving mammals.,Isogai Y, Imamura H, Nakae S, Sumi T, Takahashi KI, Shirai T iScience. 2021 Jul 30;24(8):102920. doi: 10.1016/j.isci.2021.102920. eCollection , 2021 Aug 20. PMID:34430810[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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