2AN0
Crystal Structure of the P332G mutant of the Bacillus subtilis NOS
Summary for 2AN0
| Entry DOI | 10.2210/pdb2an0/pdb |
| Related | 1M7Z 2AMO |
| Descriptor | Nitric Oxide Synthase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | p332g mutant, prokaryotic nitric oxide synthase, bacillus subtilis, oxidoreductase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 42094.03 |
| Authors | Pant, K.,Crane, B.R. (deposition date: 2005-08-10, release date: 2006-08-29, Last modification date: 2024-02-14) |
| Primary citation | Pant, K.,Crane, B.R. Structure of a loose dimer: an intermediate in nitric oxide synthase assembly J.Mol.Biol., 352:932-940, 2005 Cited by PubMed Abstract: 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. PubMed: 16126221DOI: 10.1016/j.jmb.2005.07.070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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