Premium
Crystal structure of the Agrobacterium tumefaciens type VI effector–immunity complex
Author(s) -
Fukuhara Satoshi,
Nakane Takanori,
Yamashita Keitaro,
Ishii Ryohei,
Ishitani Ryuichiro,
Nureki Osamu
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18016369
Subject(s) - agrobacterium tumefaciens , effector , periplasmic space , type vi secretion system , biology , bacteria , microbiology and biotechnology , agrobacterium , secretion , ti plasmid , immunity , amidase , transformation (genetics) , genetics , biochemistry , immune system , escherichia coli , gene , virulence
The type VI secretion system (T6SS) comprises needle‐shaped multisubunit complexes that play a role in the microbial defense systems of Gram‐negative bacteria. Some Gram‐negative bacteria harboring a T6SS deliver toxic effector proteins into the cytoplasm or periplasm of competing bacteria in order to lyse and kill them. To avoid self‐cell disruption, these bacteria have cognate immunity proteins that inhibit their toxic effector proteins. T6SS amidase effector protein 4 (Tae4) and T6SS amidase immunity protein 4 (Tai4) are a representative of the toxic effector–immunity pairs of the T6SS. Here, the three‐dimensional structures of Tai4 and the Tae4–Tai4 complex from Agrobacterium tumefaciens are reported at 1.55 and 1.9 Å resolution, respectively. A structural comparison with other Tae4–Tai4 homologs revealed similarities and differences in the catalytic and inhibitory mechanisms among the Tae4 and Tai4 family proteins.