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SUMMARY:Structural basis of specific lysine transport by Pseudomonas aerug
 inosa permease LysP
DTSTART;VALUE=DATE-TIME:20260327T114000Z
DTEND;VALUE=DATE-TIME:20260327T120000Z
DTSTAMP;VALUE=DATE-TIME:20260426T030118Z
UID:indico-contribution-10350@events.saip.org.za
DESCRIPTION:Speakers: Emmanuel  Nji (BioStruct-Africa)\nUnder conditions o
 f extreme acidity\, the lysine-specific permease\, LysP\, not only mediate
 s the import of L-lysine it also interacts with the transcriptional regula
 tor\, CadC\, to activate expression of the cadAB operon. This operon encod
 es the lysine decarboxylase\, CadA\, which converts lysine to cadaverine w
 hile consuming a cytoplasmic proton\, and the antiporter\, CadB\, which ex
 ports protonated cadaverine in exchange for extracellular lysine. Together
 \, these processes contribute to cytoplasmic pH homeostasis and support ba
 cterial acid resistance - a mechanism essential for the survival of pathog
 enic bacteria in acidic host environments. Here\, we present the cryo-EM s
 tructure of LysP from Pseudomonas aeruginosa in an inward-occluded conform
 ation (3.2–5.3 Å resolution)\, bound to L-lysine and a nanobody. L-Ly
 sine is coordinated by hydrophobic contacts\, cation–π interactions\, a
 nd by hydrogen bonding mostly with polar uncharged residues. Reconstitutio
 n of LysP into proteoliposomes confirms specific L-lysine transport\, whic
 h is competitively inhibited by L-4-thialysine. These findings provide a s
 tructural framework for understanding selective lysine recognition and inh
 ibition\, with implications for antibacterial drug design.\n\nhttps://even
 ts.saip.org.za/event/272/contributions/10350/
LOCATION:
URL:https://events.saip.org.za/event/272/contributions/10350/
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