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Near-atomic resolution analysis of BipD, a component of the type III secretion system ofBurkholderia pseudomallei

journal contribution
posted on 2023-06-09, 04:36 authored by Mohinder Pal, P T Erskine, R S Gill, S P Wood, J B Cooper
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 Å 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.

History

Publication status

  • Published

Journal

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ISSN

1744-3091

Publisher

International Union of Crystallography

Issue

9

Volume

66

Page range

990-993

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2017-01-09

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