1NOC

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114) COMPLEXED WITH TYPE I E. COLI CHLORAMPHENICOL ACETYL TRANSFERASE AND IMIDAZOLE

Summary for 1NOC

• Entry DOI: 10.2210/pdb1noc/pdb
• Descriptor: INDUCIBLE NITRIC OXIDE SYNTHASE, TYPE 1 CHLORAMPHENICOL ACETYLTRANSFERASE, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: nitric oxide, l-arginine monooxygenase, heme, imidazole, nos, no, cat, complex (oxidoreductase-transferase), complex (oxidoreductase-transferase) complex, complex (oxidoreductase/transferase)
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 71585.99

Authors

Crane, B.R.,Arvai, A.S.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A. (deposition date: 1997-09-28, release date: 1998-10-14, Last modification date: 2024-02-14)

Primary citation

Crane, B.R.,Arvai, A.S.,Gachhui, R.,Wu, C.,Ghosh, D.K.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A.
The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.
Science, 278:425-431, 1997

PubMed Abstract: The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOSox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged beta sheet engenders a curved alpha-beta domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.

PubMed: 9334294
DOI: 10.1126/science.278.5337.425

Experimental method

X-RAY DIFFRACTION (2.6 Å)