5AUR

Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region

5AUR の概要

• エントリーDOI: 10.2210/pdb5aur/pdb
• 関連するPDBエントリー: 3VYM 5AUS
• 分子名称: Cytochrome c-552, HEME C, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: electron transfer, 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: 4
• 化学式量合計: 38898.63

構造登録者

Ren, C.,Nagao, S.,Yamanaka, M.,Kamikubo, H.,Komori, H.,Shomura, Y.,Higuchi, Y.,Hirota, S. (登録日: 2015-06-08, 公開日: 2015-10-21, 最終更新日: 2024-11-13)

主引用文献

Ren, C.,Nagao, S.,Yamanaka, M.,Komori, H.,Shomura, Y.,Higuchi, Y.,Hirota, S.
Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop.
Mol Biosyst, 11:3218-3221, 2015

PubMed Abstract: High-order oligomers of Hydrogenobacter thermophilus cytochrome c552 increased with the insertion of more Gly residues between Ala18 and Lys19 at the major hinge loop of the wild-type protein. N-Terminal domain swapping and C-terminal domain swapping were elucidated by using X-ray crystallography for the mutant with the insertion of three Gly residues at the hinge loop.

PubMed: 26451671
DOI: 10.1039/c5mb00545k

実験手法

X-RAY DIFFRACTION (1.26 Å)