3NFT
Near-atomic resolution analysis of BipD- A component of the type-III secretion system of Burkholderia pseudomallei
Summary for 3NFT
Entry DOI | 10.2210/pdb3nft/pdb |
Related | 2IZP |
Descriptor | Translocator protein bipD (2 entities in total) |
Functional Keywords | virulence, translocation, transport protein |
Biological source | Burkholderia pseudomallei (Pseudomonas pseudomallei) |
Cellular location | Secreted: Q63K37 |
Total number of polymer chains | 1 |
Total formula weight | 33087.22 |
Authors | Pal, M.,Erskine, P.T.,Gill, R.S.,Wood, S.P.,Cooper, J.B. (deposition date: 2010-06-10, release date: 2010-07-14, Last modification date: 2023-09-06) |
Primary citation | Pal, M.,Erskine, P.T.,Gill, R.S.,Wood, S.P.,Cooper, J.B. Near-atomic resolution analysis of BipD, a component of the type III secretion system of Burkholderia pseudomallei. Acta Crystallogr.,Sect.F, 66:990-993, 2010 Cited by PubMed Abstract: Burkholderia pseudomallei, the causative agent of melioidosis, possesses a type III protein secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to inject virulence-associated proteins into target cells of the host organism. The bipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and is most likely to be functionally analogous to IpaD from Shigella and SipD from Salmonella. Proteins in this family are thought to act as extracellular chaperones at the tip of the secretion needle to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and may also link the translocon pore with the secretion needle. BipD has been crystallized in a monoclinic crystal form that diffracted X-rays to 1.5 A resolution and the structure was refined to an R factor of 16.1% and an Rfree of 19.8% at this resolution. The putative dimer interface that was observed in previous crystal structures was retained and a larger surface area was buried in the new crystal form. PubMed: 20823511DOI: 10.1107/S1744309110026333 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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