4ZID

Dimeric Hydrogenobacter thermophilus cytochrome c552 obtained from Escherichia coli

4ZID の概要

• エントリーDOI: 10.2210/pdb4zid/pdb
• 関連するPDBエントリー: 3VYM
• 分子名称: Cytochrome c-552, HEME C (3 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9204.52

構造登録者

Hayashi, Y.,Yamanaka, M.,Nagao, S.,Komori, H.,Higuchi, Y.,Hirota, S. (登録日: 2015-04-28, 公開日: 2016-02-10, 最終更新日: 2024-10-30)

主引用文献

Hayashi, Y.,Yamanaka, M.,Nagao, S.,Komori, H.,Higuchi, Y.,Hirota, S.
Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells
Sci Rep, 6:19334-19334, 2016

PubMed Abstract: Knowledge on domain swapping in vitro is increasing, but domain swapping may not occur regularly in vivo, and its information in cells is limited. Herein, we show that domain-swapped oligomers of a thermostable c-type cytochrome, Hydrogenobacter thermophilus cyt c552, are formed in E. coli which expresses cyt c552. The region containing the N-terminal α-helix and heme was domain-swapped between protomers in the dimer formed in E. coli. The amount of cyt c552 oligomers increased in E. coli as the cyt c552 concentration was increased, whereas that of high-order oligomers decreased in the order of decrease in protein stability, indicating that domain swapping decreases in cells when the protein stability decreases. Apo cyt c552 was detected in the cyt c552 oligomer formed in E. coli, but not in that of the A5F/M11V/Y32F/Y41E/I76V mutant. The cyt c552 oligomer containing its apo protein may form at the periplasm, since the apo protein detected by mass measurements did not contain the signal peptide. These results show that domain-swapped cyt c552 oligomers were formed in E. coli, owing to the stability of the transient oligomer containing the apo protein before heme attachment. This is an indication that exceedingly stable proteins may have disadvantages forming domain-swapped oligomers in cells.

PubMed: 26838805
DOI: 10.1038/srep19334

実験手法

X-RAY DIFFRACTION (1.8 Å)