4F0V

Crystal structure of type effector Tse1 from Pseudomonas aeruginousa

Summary for 4F0V

• Entry DOI: 10.2210/pdb4f0v/pdb
• Related: 4E0W
• Descriptor: Putative uncharacterized protein, SUCCINIC ACID (3 entities in total)
• Functional Keywords: nlpc/p60 domain, type vi amidase effector, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 20314.83

Authors

Zhang, H.,Gao, Z.Q.,Dong, Y.H. (deposition date: 2012-05-05, release date: 2012-06-27, Last modification date: 2024-11-13)

Primary citation

Zhang, H.,Gao, Z.Q.,Su, X.D.,Dong, Y.H.
Crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa.
Febs Lett., 586:3193-3199, 2012

PubMed Abstract: 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.

PubMed: 22750141
DOI: 10.1016/j.febslet.2012.06.036

Experimental method

X-RAY DIFFRACTION (1.6 Å)