Structural highlights
Publication Abstract from PubMed
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 A 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.
Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa.,Robb CS, Assmus M, Nano FE, Boraston AB Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):607-10. doi: , 10.1107/S1744309113012220. Epub 2013 May 23. PMID:23722835[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Robb CS, Assmus M, Nano FE, Boraston AB. Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):607-10. doi: , 10.1107/S1744309113012220. Epub 2013 May 23. PMID:23722835 doi:10.1107/S1744309113012220
