Protein Family Models

The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. This domain represents the PE domain located at the N-terminal region of EspB which carries the conserved YxxxD/E secretion motif [1]. [1]. 26051906. Structure of EspB, a secreted substrate of the ESX-1 secretion system of Mycobacterium tuberculosis. Korotkova N, Piton J, Wagner JM, Boy-Rottger S, Japaridze A, Evans TJ, Cole ST, Pojer F, Korotkov KV;. J Struct Biol. 2015;191:236-244. (from Pfam)

Date:

2024-10-16

This entry represents the PPe domain of ESX-1 secretion- associated protein EspB, a member of the PE/PPE family and the only one described to date to form higher-order oligomers [1-3]. It contains PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. EspB oligomerises into a cylinder-like heptamer through its N-terminal domain, that form channel-like structures [1-3]. [1]. 32875288. High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis. Piton J, Pojer F, Wakatsuki S, Gati C, Cole ST;. J Struct Biol X. 2020;4:100029. [2]. 36463964. The crystal structure of the EspB-EspK virulence factor-chaperone complex suggests an additional type VII secretion mechanism in Mycobacterium tuberculosis. Gijsbers A, Eymery M, Gao Y, Menart I, Vinciauskaite V, Siliqi D, Peters PJ, McCarthy A, Ravelli RBG;. J Biol Chem. 2023;299:102761. [3]. 34337436. Priming mycobacterial ESX-secreted protein B to form a channel-like structure. Gijsbers A, Vinciauskaite V, Siroy A, Gao Y, Tria G, Mathew A, Sanchez-Puig N, Lopez-Iglesias C, Peters PJ, Ravelli RBG;. Curr Res Struct Biol. 2021;3:153-164. (from Pfam)

Date:

2024-10-29