Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa. Issue 6 (31st May 2013)

• Record Type: Journal Article
• Authors: Robb, Craig S.; Assmus, Mark; Nano, Francis E.; Boraston, Alisdair B.
• Is Part Of: Acta crystallographica. Volume 69:Issue 6(2013:Jun.)
• Page Start: 607
• Page End: 610
• Publication Date: 2013-05-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113012220
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The type VI secretion system of <italic>Pseudomonas aeruginosa</italic> 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 <italic>Escherichia coli</italic> and <italic>Serratia marcescens</italic> have been published. Here, the X‐ray crystal structure of TssJ1 from <italic>P. aeruginosa</italic> 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.</p> </abstract>