5YCG

Ancestral myoglobin aMbWp of Pakicetus relative

Summary for 5YCG

• Entry DOI: 10.2210/pdb5ycg/pdb
• Related: 5YCE
• Descriptor: Ancestral myoglobin aMbWp of Pakicetus relative, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: globin, molecular archaeology, ancient protein, protein evolution, deep-sea adaptation, oxygen storage
• Biological source: Physeter catodon
• Total number of polymer chains: 1
• Total formula weight: 18046.44

Authors

Isogai, Y.,Imamura, H.,Nakae, S.,Sumi, T.,Takahashi, K.,Nakagawa, T.,Tsuneshige, A.,Shirai, T. (deposition date: 2017-09-07, release date: 2018-09-19, Last modification date: 2023-11-22)

Primary citation

Isogai, Y.,Imamura, H.,Nakae, S.,Sumi, T.,Takahashi, K.I.,Nakagawa, T.,Tsuneshige, A.,Shirai, T.
Tracing whale myoglobin evolution by resurrecting ancient proteins.
Sci Rep, 8:16883-16883, 2018

PubMed Abstract: 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.

PubMed: 30442991
DOI: 10.1038/s41598-018-34984-6

Experimental method

X-RAY DIFFRACTION (2.4 Å)