2AN0

Crystal Structure of the P332G mutant of the Bacillus subtilis NOS

2AN0 の概要

• エントリーDOI: 10.2210/pdb2an0/pdb
• 関連するPDBエントリー: 1M7Z 2AMO
• 分子名称: Nitric Oxide Synthase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: p332g mutant, prokaryotic nitric oxide synthase, bacillus subtilis, oxidoreductase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42094.03

構造登録者

Pant, K.,Crane, B.R. (登録日: 2005-08-10, 公開日: 2006-08-29, 最終更新日: 2024-02-14)

主引用文献

Pant, K.,Crane, B.R.
Structure of a loose dimer: an intermediate in nitric oxide synthase assembly
J.Mol.Biol., 352:932-940, 2005

PubMed Abstract: Cooperativity among ligand binding, subunit association, and protein folding has implications for enzyme regulation as well as protein aggregation events associated with disease. The binding of substrate l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases (NOSs) from a "loose dimer", with an exposed active center and higher sensitivity to proteolysis, to a "tight dimer" competent for catalysis. The crystallographic structure of the Bacillus subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains. Ligand binding or heme reduction converts loose dimers to tight dimers in solution and crystals. Mutations at key positions in the dimer interface that distinguish prokaryotic from eukaryotic NOSs affect the propensity to form loose dimers. The loose dimer structure indicates that non-native interactions can mediate subunit association in NOS.

PubMed: 16126221
DOI: 10.1016/j.jmb.2005.07.070

実験手法

X-RAY DIFFRACTION (2.6 Å)