5I5I

Shewanella denitrificans nitrous oxide reductase, app form

5I5I の概要

• エントリーDOI: 10.2210/pdb5i5i/pdb
• 分子名称: Nitrous-oxide reductase (2 entities in total)
• 機能のキーワード: nitrogen cycle nitrous oxide reductase beta propeller apoprotein, oxidoreductase
• 由来する生物種: Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141918.91

構造登録者

Schneider, L.K.,Einsle, O. (登録日: 2016-02-15, 公開日: 2016-03-02, 最終更新日: 2024-10-23)

主引用文献

Schneider, L.K.,Einsle, O.
Role of Calcium in Secondary Structure Stabilization during Maturation of Nitrous Oxide Reductase.
Biochemistry, 55:1433-1440, 2016

PubMed Abstract: The copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide N₂O to dinitrogen N₂. Its maturation largely occurs in the periplasm and includes the insertion of at least one Ca²⁺ ion per monomer. Here we have investigated the role of this structural cation in recombinantly produced apo-N₂OR from Shewanella denitrificans and have determined the three-dimensional structure of the protein by X-ray crystallography. In the absence of Ca²⁺, substantial parts of the enzyme surrounding the binding sites for the copper ions show structural disorder. Reconstitution of the binuclear CuA site was possible in vitro but required the presence of Ca²⁺ ions for a stable insertion of the center. In contrast, an excess of Ca²⁺ prevented copper insertion, and the structural analysis of the Ca²⁺apo form revealed that the cation is sufficient to structure the disordered regions of the protein even in the absence of Cu ions, indicating that the geometry of the two noncanonical copper centers is largely predetermined by the protein structure.

PubMed: 26885878
DOI: 10.1021/acs.biochem.5b01278

実験手法

X-RAY DIFFRACTION (2.14 Å)