5D5R

Horse-heart myoglobin - deoxy state

5D5R の概要

• エントリーDOI: 10.2210/pdb5d5r/pdb
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: myoglobin, heme protein, oxygen storage
• 由来する生物種: Equus caballus (Horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17542.95

構造登録者

Barends, T.,Schlichting, I. (登録日: 2015-08-11, 公開日: 2015-09-16, 最終更新日: 2024-01-10)

主引用文献

Barends, T.R.,Foucar, L.,Ardevol, A.,Nass, K.,Aquila, A.,Botha, S.,Doak, R.B.,Falahati, K.,Hartmann, E.,Hilpert, M.,Heinz, M.,Hoffmann, M.C.,Kofinger, J.,Koglin, J.E.,Kovacsova, G.,Liang, M.,Milathianaki, D.,Lemke, H.T.,Reinstein, J.,Roome, C.M.,Shoeman, R.L.,Williams, G.J.,Burghardt, I.,Hummer, G.,Boutet, S.,Schlichting, I.
Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation.
Science, 350:445-450, 2015

PubMed Abstract: The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein.

PubMed: 26359336
DOI: 10.1126/science.aac5492

実験手法

X-RAY DIFFRACTION (1.6 Å)