3WIA

Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase

3WIA の概要

• エントリーDOI: 10.2210/pdb3wia/pdb
• 関連するPDBエントリー: 3WI9
• 分子名称: Nitrite reductase, COPPER (II) ION, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: cupredoxin-fold, trimer, nitrite reduction, oxidoreductase
• 由来する生物種: Geobacillus kaustophilus
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 287197.92

構造登録者

Fukuda, Y.,Nojiri, M. (登録日: 2013-09-09, 公開日: 2014-07-23, 最終更新日: 2023-11-08)

主引用文献

Fukuda, Y.,Koteishi, H.,Yoneda, R.,Tamada, T.,Takami, H.,Inoue, T.,Nojiri, M.
Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner
Biochim.Biophys.Acta, 1837:396-405, 2014

PubMed Abstract: The crystal structures of copper-containing nitrite reductase (CuNiR) from the thermophilic Gram-positive bacterium Geobacillus kaustophilus HTA426 and the amino (N)-terminal 68 residue-deleted mutant were determined at resolutions of 1.3Å and 1.8Å, respectively. Both structures show a striking resemblance with the overall structure of the well-known CuNiRs composed of two Greek key β-barrel domains; however, a remarkable structural difference was found in the N-terminal region. The unique region has one β-strand and one α-helix extended to the northern surface of the type-1 copper site. The superposition of the Geobacillus CuNiR model on the electron-transfer complex structure of CuNiR with the redox partner cytochrome c551 in other denitrifier system led us to infer that this region contributes to the transient binding with the partner protein during the interprotein electron transfer reaction in the Geobacillus system. Furthermore, electron-transfer kinetics experiments using N-terminal residue-deleted mutant and the redox partner, Geobacillus cytochrome c551, were carried out. These structural and kinetics studies demonstrate that the region is directly involved in the specific partner recognition.

PubMed: 24440558
DOI: 10.1016/j.bbabio.2014.01.004

実験手法

X-RAY DIFFRACTION (1.77 Å)