1ABS

PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K

1ABS の概要

• エントリーDOI: 10.2210/pdb1abs/pdb
• 分子名称: MYOGLOBIN, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: oxygen storage, intermediate in ligand binding, respiratory protein
• 由来する生物種: Physeter catodon (sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18105.72

構造登録者

Schlichting, I.,Berendzen, J.,Phillips Jr., G.N.,Sweet, R.M. (登録日: 1997-01-28, 公開日: 1997-04-01, 最終更新日: 2024-05-22)

主引用文献

Schlichting, I.,Berendzen, J.,Phillips Jr., G.N.,Sweet, R.M.
Crystal structure of photolysed carbonmonoxy-myoglobin.
Nature, 371:808-812, 1994

PubMed Abstract: Myoglobin is a globular haem protein that reversibly binds ligands such as O2 and CO. Single photons of visible light can break the covalent bond between CO and the haem iron in carbon-monoxy-myoglobin (MbCO) and thus form an unstable intermediate, Mb*CO, with the CO inside the protein. The ensuing rebinding process has been extensively studied as a model for the interplay of dynamics, structure and function in protein reactions. We have used X-ray crystallography at liquid-helium temperatures to determine the structure of Mb*CO to a resolution of 1.5 A. The photodissociated CO lies on top of the haem pyrrole ring C. Comparison with the CO-bound and unligated myoglobin structures reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haem plane, the iron-proximal histidine bonds is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket.

PubMed: 7935843
DOI: 10.1038/371808a0

実験手法

X-RAY DIFFRACTION (1.5 Å)