6BR4
Crystal structure of Escherichia coli DsbA in complex with {N}-methyl-1-(3-thiophen-2-ylphenyl)methanamine
Summary for 6BR4
| Entry DOI | 10.2210/pdb6br4/pdb |
| Related | 4wf5 |
| Descriptor | Thiol:disulfide interchange protein DsbA, ~{N}-methyl-1-(3-thiophen-2-ylphenyl)methanamine, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | disulphide catalysts, thiol oxidase, virulence factor foldase, oxidoreductase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 2 |
| Total formula weight | 42640.44 |
| Authors | Heras, B.,Totsika, M.,Paxman, J.J.,Wang, G.,Scanlon, M.J.,Martin, J.L. (deposition date: 2017-11-29, release date: 2017-12-27, Last modification date: 2024-11-20) |
| 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 Cited by 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: 29237285DOI: 10.1089/ars.2017.7104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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