7DDR

Ancestral myoglobin aMbSp of Puijila Darwini relative (imidazol ligand)

Summary for 7DDR

• Entry DOI: 10.2210/pdb7ddr/pdb
• Descriptor: Ancestral myoglobin aMbSp, PROTOPORPHYRIN IX CONTAINING FE, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: protein evolution, ancestral protein, diving adaptation, seals, oxygen storage
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 17842.34

Authors

Isogai, Y.,Imamura, H.,Nakae, S.,Sumi, T.,Takahashi, K.,Shirai, T. (deposition date: 2020-10-29, release date: 2021-09-08, Last modification date: 2023-11-29)

Primary citation

Isogai, Y.,Imamura, H.,Nakae, S.,Sumi, T.,Takahashi, K.I.,Shirai, T.
Common and unique strategies of myoglobin evolution for deep-sea adaptation of diving mammals.
Iscience, 24:102920-102920, 2021

PubMed Abstract: 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.

PubMed: 34430810
DOI: 10.1016/j.isci.2021.102920

Experimental method

X-RAY DIFFRACTION (1.5 Å)