2IXR
BipD of Burkholderia Pseudomallei
Summary for 2IXR
| Entry DOI | 10.2210/pdb2ixr/pdb |
| Related | 2CMQ 2IZP |
| Descriptor | MEMBRANE ANTIGEN (2 entities in total) |
| Functional Keywords | burkholderia pseudomallei, toxin, bipd, ttss, t3ss, type 3 secretion system |
| Biological source | BURKHOLDERIA PSEUDOMALLEI |
| Cellular location | Secreted: Q63K37 |
| Total number of polymer chains | 1 |
| Total formula weight | 33087.22 |
| Authors | Roversi, P.,Johnson, S.,Field, T.,Deane, J.E.,Galyov, E.E.,Lea, S.M. (deposition date: 2006-07-10, release date: 2006-11-02, Last modification date: 2024-05-08) |
| Primary citation | Johnson, S.,Roversi, P.,Espina, M.,Olive, A.,Deane, J.E.,Birket, S.,Field, T.,Picking, W.D.,Blocker, A.J.,Galyov, E.E.,Picking, W.L.,Lea, S.M. Self-Chaperoning of the Type III Secretion System Needle Tip Proteins Ipad and Bipd. J.Biol.Chem., 282:4035-, 2007 Cited by PubMed Abstract: Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure. PubMed: 17077085DOI: 10.1074/JBC.M607945200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
