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Crystal structure of the type VI effector-immunity complex (Tae4-Tai4) from Agrobacterium tumefaciensCrystal structure of the type VI effector-immunity complex (Tae4-Tai4) from Agrobacterium tumefaciens
Structural highlights
FunctionPublication Abstract from PubMedThe 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 A 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. Crystal structure of the Agrobacterium tumefaciens type VI effector-immunity complex.,Fukuhara S, Nakane T, Yamashita K, Ishii R, Ishitani R, Nureki O Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):810-816. doi:, 10.1107/S2053230X18016369. Epub 2018 Nov 30. PMID:30511676[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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