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Lookup NU author(s): Professor Alastair Hawkins
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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 SANDS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 Angstrom. Haem and S-ethylisothiourea (SEITU) are bound at the SANDS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H4B) in mammalian NOSs, has NAD+ bound in SANDS. In common with all bacterial NOSs, SANDS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.
Author(s): Hawkins AR; Bird LE; Ren JS; Zhang JC; Foxwell N; Charles IG; Stammers DK
Publication type: Article
Publication status: Published
Journal: Structure
Year: 2002
Volume: 10
Issue: 12
Pages: 1687-1696
ISSN (print): 0969-2126
ISSN (electronic): 1878-4186
Publisher: Cell Press
URL: http://dx.doi.org/10.1016/S0969-2126(02)00911-5
DOI: 10.1016/S0969-2126(02)00911-5
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