Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3NFT

Near-atomic resolution analysis of BipD- A component of the type-III secretion system of Burkholderia pseudomallei

Summary for 3NFT
Entry DOI10.2210/pdb3nft/pdb
Related2IZP
DescriptorTranslocator protein bipD (2 entities in total)
Functional Keywordsvirulence, translocation, transport protein
Biological sourceBurkholderia pseudomallei (Pseudomonas pseudomallei)
Cellular locationSecreted: Q63K37
Total number of polymer chains1
Total formula weight33087.22
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 citationPal, 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: 20823511
DOI: 10.1107/S1744309110026333
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.51 Å)
Structure validation

239149

數據於2025-07-23公開中

PDB statisticsPDBj update infoContact PDBjnumon