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Crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa
Author(s) -
Zhang Heng,
Gao Zeng-Qiang,
Su Xiao-Dong,
Dong Yu-Hui
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.036
Subject(s) - periplasmic space , peptidoglycan , pseudomonas aeruginosa , amidase , type vi secretion system , secretion , chemistry , microbiology and biotechnology , residue (chemistry) , effector , bacteria , biology , biochemistry , enzyme , escherichia coli , genetics , virulence , gene
The type VI secretion systems (T6SS) have emerging roles in interspecies competition. In order to have an advantage in defense against other organisms, this system in Pseudomonas aeruginosa delivers a peptidoglycan amidase (Tse1) to the periplasmic space of a competitor. An immune protein (Tsi1) is also produced by the bacterium to protect itself from damage caused by Tse1. Tsi1 directly interacts with Tse1. We report that the crystal structure of Tse1 displays a common CHAP protein fold. Strikingly, our structures showed that the third residue in the catalytic triad may be novel as this residue type has not been observed previously.