2an2

P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase

spinqualitylabelsall models 2an2, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2an2 is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: ARG, H4B, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NOSO_BACSU Catalyzes the production of nitric oxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of a loose dimer: an intermediate in nitric oxide synthase assembly.,Pant K, Crane BR J Mol Biol. 2005 Sep 30;352(4):932-40. PMID:16126221 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitric Oxide Synthase 3D structures

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