1MJT

CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU

1MJT の概要

• エントリーDOI: 10.2210/pdb1mjt/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: NITRIC-OXIDE SYNTHASE HOMOLOG, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• 機能のキーワード: sanos, no, nos, bacterial, staphylococcus aureus, synthase, mrsa, seitu, oxidoreductase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84480.20

構造登録者

Bird, L.E.,Ren, J.,Stammers, D.K. (登録日: 2002-08-28, 公開日: 2003-01-07, 最終更新日: 2024-02-14)

主引用文献

Bird, L.E.,Ren, J.,Zhang, J.,Foxwell, N.,Hawkins, A.R.,Charles, I.G.,Stammers, D.K.
Crystal Structure of SANOS, a Bacterial Nitric Oxide Synthase Oxygenase Protein from Staphylococcus aureus
Structure, 10:1687-1696, 2002

PubMed Abstract: Prokaryotic genes related to the oxygenase domain of mammalian nitric oxide synthases (NOSs) have recently been identified. Although they catalyze the same reaction as the eukaryotic NOS oxygenase domain, their biological function(s) are unknown. In order to explore rationally the biochemistry and evolution of the prokaryotic NOS family, we have determined the crystal structure of SANOS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.

PubMed: 12467576
DOI: 10.1016/S0969-2126(02)00911-5

実験手法

X-RAY DIFFRACTION (2.4 Å)