Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa

Craig S. Robb, Mark Assmus, Francis E. Nano, Alisdair B. Boraston*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The type VI secretion system of Pseudomonas aeruginosa has been shown to be responsible for the translocation of bacteriolytic effectors into competing bacteria. A mechanistic understanding of this widely distributed secretion system is developing and structural studies of its components are ongoing. Two representative structures of one highly conserved component, TssJ, from Escherichia coli and Serratia marcescens have been published. Here, the X-ray crystal structure of TssJ1 from P. aeruginosa is presented at 1.4 Å resolution. The overall structure is conserved among the three proteins. This finding suggests that the homologues function in a similar manner and bolsters the understanding of the structure of this family of proteins.

Original languageEnglish (US)
Pages (from-to)607-610
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number6
DOIs
StatePublished - 2013
Externally publishedYes

Keywords

  • Pseudomonas aeruginosa
  • T6SS
  • TssJ1
  • lipoproteins

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint

Dive into the research topics of 'Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa'. Together they form a unique fingerprint.

Cite this