1MJT

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

Summary for 1MJT

• Entry DOI: 10.2210/pdb1mjt/pdb
• Related PRD ID: PRD_900003
• Descriptor: NITRIC-OXIDE SYNTHASE HOMOLOG, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: sanos, no, nos, bacterial, staphylococcus aureus, synthase, mrsa, seitu, oxidoreductase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 84480.20

Authors

Bird, L.E.,Ren, J.,Stammers, D.K. (deposition date: 2002-08-28, release date: 2003-01-07, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)