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OprG is an outer membrane protein of Pseudomonas aeruginosa whose function as an antibiotic-sensitive porin has been controversial and not well defined. Circumstantial evidence led to the proposal that OprG might transport hydrophobic compounds by using a lateral gate in the barrel wall thought to be lined by three conserved prolines. To test this hypothesis and to find the physiological substrates...
Nuclear magnetic resonance (NMR) studies on an HIV gp41 construct reported by Lakomek and colleagues in this issue of Structure have revealed the conformational dynamics of a possible trimeric prehairpin fusion intermediate and its interactions with lipids. Two alternative fusion pathways are compared based on this work and a previous NMR structure of a monomeric lipid-bound gp41 ectodomain construct.
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