| Structural highlights
5g6c is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Related: | 5g65, 5g66, 5g67, 5g68, 5g69, 5g6a, 5g6b, 5g6d, 5g6e, 5g6f, 5g6g, 5g6h, 5g6i, 5g6j, 5g6k, 5g6l, 5g6m, 5g6n, 5g6o, 5g6p, 5g6q |
| Activity: | Nitric-oxide synthase (NAD(P)H-dependent), with EC number 1.14.13.165 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NOSO_BACSU] Catalyzes the production of nitric oxide.
Publication Abstract from PubMed
Nitric oxide (NO) is produced in Gram-positive pathogens Bacillus anthracis and Staphylococcus aureus by the bacterial isoform of nitric oxide synthase (NOS). Inhibition of bacterial nitric oxide synthase (bNOS) has been identified as a promising antibacterial strategy for targeting methicillin-resistant Staphylocoocus aureus1. One class of NOS inhibitors that demonstrates antimicrobial efficacy utilizes an aminoquinoline scaffold. Here we report on a variety of aminoquinolines that target the bacterial NOS active site, in part, by binding to a hydrophobic patch that is unique to bNOS. Through mutagenesis and crystallographic studies, our findings demonstrate that aminoquinolines are an excellent scaffold to further aid in the development of bNOS-specific inhibitors.
Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-based Inhibitors.,Holden JK, Lewis MC, Cinelli MA, Abdullatif Z, Pensa AV, Silverman RB, Poulos TL Biochemistry. 2016 Sep 8. PMID:27607918[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Holden JK, Lewis MC, Cinelli MA, Abdullatif Z, Pensa AV, Silverman RB, Poulos TL. Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-based Inhibitors. Biochemistry. 2016 Sep 8. PMID:27607918 doi:http://dx.doi.org/10.1021/acs.biochem.6b00786
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