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- W3044972614 endingPage "183412" @default.
- W3044972614 startingPage "183412" @default.
- W3044972614 abstract "Mannose transporters constitute a superfamily (Man-PTS) of the Phosphoenolpyruvate Carbohydrate Phosphotransferase System (PTS). The membrane complexes are homotrimers of protomers consisting of two subunits, IIC and IID. The two subunits without recognizable sequence similarity assume the same fold, and in the protomer are structurally related by a two fold pseudosymmetry axis parallel to membrane-plane (Liu et al. (2019) Cell Research 29 680). Two reentrant loops and two transmembrane helices of each subunit together form the N-terminal transport domain. Two three-helix bundles, one of each subunit, form the scaffold domain. The protomer is stabilized by a helix swap between these bundles. The two C-terminal helices of IIC mediate the interprotomer contacts. PTS occur in bacteria and archaea but not in eukaryotes. Man-PTS are abundant in Gram-positive bacteria living on carbohydrate rich mucosal surfaces. A subgroup of IICIID complexes serve as receptors for class IIa bacteriocins and as channel for the penetration of bacteriophage lambda DNA across the inner membrane. Some Man-PTS are associated with host-pathogen and -symbiont processes. • Sugar transport protein with novel fold and subunit composition • Present in bacteria and archaea with up to 27 paralogs per genome • “Open door” for bacteriocins and phage DNA • Comprehensive review on the Mannose-phosphotransferase system (Man-PTS)" @default.
- W3044972614 created "2020-07-29" @default.
- W3044972614 creator A5049957563 @default.
- W3044972614 creator A5066076108 @default.
- W3044972614 date "2020-11-01" @default.
- W3044972614 modified "2023-09-26" @default.
- W3044972614 title "The mannose phosphotransferase system (Man-PTS) - Mannose transporter and receptor for bacteriocins and bacteriophages" @default.
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