9RC4
Crystal structure of VirJ domain 1 from Brucella
Summary for 9RC4
| Entry DOI | 10.2210/pdb9rc4/pdb |
| Descriptor | Virulence factor family protein, GLYCEROL (3 entities in total) |
| Functional Keywords | brucella, type iv secretion, membrane, phosphatidyl glycerol, transferase |
| Biological source | Brucella abortus |
| Total number of polymer chains | 2 |
| Total formula weight | 48445.05 |
| Authors | Dugelay, C.,Ferrarin, S.,Terradot, L. (deposition date: 2025-05-27, release date: 2025-09-03, Last modification date: 2025-09-10) |
| Primary citation | Dugelay, C.,Ferrarin, S.,Terradot, L. Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus. Acta Crystallogr.,Sect.F, 81:374-380, 2025 Cited by PubMed Abstract: Virulence protein J (VirJ) is a periplasmic protein encoded by the bacterial pathogen Brucella abortus and is important for its virulence. The VirJ homologue AcvB from Agrobacterium tumefaciens was found to be a lysyl-phosphatidylglycerol hydrolase that contains two domains, D1 and D2. Interestingly, both VirJ and AcvB are associated with the type IV secretion system (T4SS) activity in the respective bacteria. To date, no structural information is available for these proteins, limiting our understanding of their function. Here, we have purified, crystallized and determined the crystal structure of the N-terminal domain 1 of VirJ (VirJ) at a resolution of 1.7 Å. Our structural analysis shows that VirJ adopts an α/β-hydrolase fold but lacks the characteristic catalytic triad. The structure presented here may help to decipher the function of VirJ in Brucella spp. and other bacterial pathogens, as well as its contribution to the T4SS function. PubMed: 40824293DOI: 10.1107/S2053230X25006697 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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