6BQX

Crystal structure of Escherichia coli DsbA in complex with N-methyl-1-(4-phenoxyphenyl)methanamine

Summary for 6BQX

• Entry DOI: 10.2210/pdb6bqx/pdb
• Descriptor: Thiol:disulfide interchange protein DsbA, N-methyl-1-(4-phenoxyphenyl)methanamine (3 entities in total)
• Functional Keywords: disulphide catalysts, thiol oxidase, virulence factor foldase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 42523.33

Authors

Heras, B.,Totsika, M.,Paxman, J.J.,Wang, G.,Scanlon, M.J. (deposition date: 2017-11-29, release date: 2017-12-27, Last modification date: 2024-11-06)

Primary citation

Totsika, M.,Vagenas, D.,Paxman, J.J.,Wang, G.,Dhouib, R.,Sharma, P.,Martin, J.L.,Scanlon, M.J.,Heras, B.
Inhibition of Diverse DsbA Enzymes in Multi-DsbA Encoding Pathogens.
Antioxid. Redox Signal., 29:653-666, 2018

PubMed Abstract: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in bacteria. In pathogens, DsbA is a major facilitator of virulence constituting a target for antivirulence antimicrobial development. However, many pathogens encode multiple and diverse DsbA enzymes for virulence factor folding during infection. The aim of this study was to determine whether our recently identified inhibitors of Escherichia coli K-12 DsbA can inhibit the diverse DsbA enzymes found in two important human pathogens and attenuate their virulence.

PubMed: 29237285
DOI: 10.1089/ars.2017.7104

Experimental method

X-RAY DIFFRACTION (1.992 Å)