5B3P

Nqo5 of the trypsin-resistant fragment (1-134) in P212121 form

5B3P の概要

• エントリーDOI: 10.2210/pdb5b3p/pdb
• 関連するPDBエントリー: 5B3Q
• 分子名称: NADH-quinone oxidoreductase subunit 5, CALCIUM ION (3 entities in total)
• 機能のキーワード: nadh-ubiquinone oxidoreductase, complex i, oxidoreductase
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15767.00

構造登録者

Hanazono, Y.,Takeda, K.,Miki, K. (登録日: 2016-03-09, 公開日: 2016-07-27, 最終更新日: 2024-03-20)

主引用文献

Hanazono, Y.,Takeda, K.,Miki, K.
Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
Febs Open Bio, 6:687-695, 2016

PubMed Abstract: The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states.

PubMed: 27398308
DOI: 10.1002/2211-5463.12070

実験手法

X-RAY DIFFRACTION (1.652 Å)