3NFT

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

3NFT の概要

• エントリーDOI: 10.2210/pdb3nft/pdb
• 関連するPDBエントリー: 2IZP
• 分子名称: Translocator protein bipD (2 entities in total)
• 機能のキーワード: virulence, translocation, transport protein
• 由来する生物種: Burkholderia pseudomallei (Pseudomonas pseudomallei)
• 細胞内の位置: Secreted: Q63K37
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33087.22

構造登録者

Pal, M.,Erskine, P.T.,Gill, R.S.,Wood, S.P.,Cooper, J.B. (登録日: 2010-06-10, 公開日: 2010-07-14, 最終更新日: 2023-09-06)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.51 Å)