State Key Laboratory of Protein and Plant Gene Research, and Biodynamic Optical Imaging Center (BIOPIC), School of Life Sciences, Peking University, Beijing 100871, China.
FEBS Lett. 2012 Sep 21;586(19):3193-9. doi: 10.1016/j.febslet.2012.06.036. Epub 2012 Jun 29.
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.
VI 型分泌系统（T6SS）在种间竞争中具有重要作用。为了在防御其他生物方面具有优势，铜绿假单胞菌中的该系统将肽聚糖酰胺酶（Tse1）输送到竞争者的周质空间。该细菌还产生一种免疫蛋白（Tsi1）来保护自身免受 Tse1 造成的损伤。Tsi1 与 Tse1 直接相互作用。我们报告称，Tse1 的晶体结构显示出常见的 CHAP 蛋白折叠。引人注目的是，我们的结构表明催化三联体中的第三个残基可能是新的，因为以前没有观察到这种残基类型。
