1LFM

CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)

1LFM の概要

• エントリーDOI: 10.2210/pdb1lfm/pdb
• 関連するPDBエントリー: 1I54 1I55 3CYT 5CYT
• 分子名称: CYTOCHROME C, PROTOPORPHYRIN IX CONTAINING CO (3 entities in total)
• 機能のキーワード: cytochrome c, folding, intermediates, electron transport
• 由来する生物種: Thunnus thynnus (bluefin tuna)
• 細胞内の位置: Mitochondrion matrix: P81459
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24019.30

構造登録者

Tezcan, F.A.,Findley, W.M.,Crane, B.R.,Ross, S.A.,Lyubovitsky, J.G.,Gray, H.B.,Winkler, J.R. (登録日: 2002-04-11, 公開日: 2002-07-19, 最終更新日: 2023-08-16)

主引用文献

Tezcan, F.A.,Findley, W.M.,Crane, B.R.,Ross, S.A.,Lyubovitsky, J.G.,Gray, H.B.,Winkler, J.R.
Using deeply trapped intermediates to map the cytochrome c folding landscape.
Proc.Natl.Acad.Sci.USA, 99:8626-8630, 2002

PubMed Abstract: Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Remarkably, neither the protein structure nor the folding thermodynamics is perturbed by this metal-ion substitution, as shown by data from spectroscopic and x-ray diffraction experiments. Through kinetics measurements, we have found parallel folding pathways involving several different misligated Co(III) species, and, as these folding intermediates persist for several hours under certain conditions, we have been able to elucidate fully their spectroscopic properties. The results, along with an analysis of the fluorescence energy-transfer kinetics during refolding, show that rapidly equilibrating populations of compact and extended polypeptide conformations are present until all molecules have reached the native structure. These measurements provide direct evidence that collapsed denatured structures are not substantially more stable than extended conformations of cytochrome c.

PubMed: 12084923
DOI: 10.1073/pnas.132254499

実験手法

X-RAY DIFFRACTION (1.5 Å)