doi: 10.1038/s41421-021-00253-6.
Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin
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- PMID:33820910
- PMCID: PMC8021565
- DOI: 10.1038/s41421-021-00253-6
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Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin
Kai Huang et al. Cell Discov..
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The authors declare no competing interests.
Figures
a The structure of the MccE492–ManYZ trimer is shown in both cartoon and surface representations as viewed from the extracellular side of the membrane. MccE492s are colored yellow, except one rainbow-colored, with its N terminus in blue and its C terminus in red, and the posttranslational modification with a salmonchelin at the C-terminus is schematically shown in red.b The perpendicular view is shown, with the white promotor omitted for clarity. The gray rectangle shows the approximate location of the inner membrane (IM).c Interactions between ManYZ and man-PTS recognition domain of MccE492. Left: surface representation of ManYZ. The man-PTS recognition domain of MccE492 is shown in sticks. Δ72–84 truncation is indicated with a scissor. Right: the same orientation and representation, except the ManYZ in cartoon representation, with key residues emphasized. The hydrogen bonds are indicated with the black dash line.d Bactericidal activity of endogenous full-length and C-terminally truncated or mutated MceA. Serial dilutions of overnight cultures were spotted (5 µl) on LB plates without IPTG (left) or with 0.2% IPTG (right).e Interactions between ManYZ and α-helical domain of MccE492. The α-helical domain of MccE492 is shown in the cartoon, with side chains represented in sticks. Mutated residues in the inhibitory assay of Mcc24 are shown as spheres. Substitutions are indicated in the circles and colored white and blue in the size of the zone of inhibition.f Model of the mechanism of MccE492 antibacterial action. Left: it is proposed that the oligomerization interface of the ManYZ complex may be the λ DNA tunnel for bacteriophage infection. Therefore, MccE492’s association with ManYZ would not affect bacteriophage λ infection. Right: postmodification by salmonchelin-like molecules at the C terminus of MccE492 is recognized by the outer membrane proteins, FepA, Fiu, and Cir for the transportation from the extracellular medium to the periplasm. The man-PTS recognition domain is then specifically docked into the pocket between Core and Vmotif domain while ManYZ occurs in the occluded state. The man-PTS recognition domain then drives the membrane insertion of the α-helical domain. Pore formation is followed by oligomerization of additional MccE492’s.
References
- Rebuffat S. Bacteriocins from gram-negative bacteria: a classification? (eds Drider D., Rebuffat S.)Prokaryotic Antimicrobial Peptides (Springer, New York, NY, 2011).
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