4K2D
Crystal structure of Burkholderia Pseudomallei DsbA
Summary for 4K2D
| Entry DOI | 10.2210/pdb4k2d/pdb |
| Descriptor | Thiol:disulfide interchange protein, GLYCEROL (3 entities in total) |
| Functional Keywords | thioredoxin fold, disulfide oxidoreductase, oxidoreductase |
| Biological source | Burkholderia pseudomallei |
| Cellular location | Periplasm (By similarity): Q63Y08 |
| Total number of polymer chains | 1 |
| Total formula weight | 22298.40 |
| Authors | McMahon, R.M. (deposition date: 2013-04-09, release date: 2013-08-14, Last modification date: 2024-10-30) |
| Primary citation | Ireland, P.M.,McMahon, R.M.,Marshall, L.E.,Halili, M.,Furlong, E.,Tay, S.,Martin, J.L.,Sarkar-Tyson, M. Disarming Burkholderia pseudomallei: Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In Vivo. Antioxid Redox Signal, 20:606-617, 2014 Cited by PubMed Abstract: The intracellular pathogen Burkholderia pseudomallei causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern Australia. The need to develop novel antimicrobials is compounded by the absence of a licensed vaccine and the bacterium's resistance to multiple antibiotics. In a number of clinically relevant Gram-negative pathogens, DsbA is the primary disulfide oxidoreductase responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins. In this study, a putative B. pseudomallei dsbA gene was evaluated functionally and structurally and its contribution to infection assessed. PubMed: 23901809DOI: 10.1089/ars.2013.5375 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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