Literature summary for 1.14.14.47 extracted from

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

Search for more literature for 1.14.14.47

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
binding of substrate L-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthase from a loose dimer, with an exposed active center and higher sensitivity to proteolysis, to a tight dimer competent for catalysis	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
P332G	mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type	Bacillus subtilis
P332G/A333S	mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O34453	-	-
Bacillus subtilis 168	O34453	-	-

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Release 2023.1 (January 2023)