The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm.
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A directly characterized Pseudomonas ortholog binds and carries multiple glycerophospholipid species.
"In Pseudomonas aeruginosa, Ttg2D is the soluble periplasmic phospholipid-binding component of an ABC transport system thought to be involved in maintaining the asymmetry of the outer membrane."
UniProt record for Pseudomonas putida KT2440 Ttg2D (Q88P91)
OpenScientist functional research for PSEPK ttg2D
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Apo and lipid-bound crystal structures exist for Q88P91 itself, directly supporting a cavity-bearing lipid-carrier architecture.
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Quantitative two-diacyl-phospholipid or one-cardiolipin loading and broad lipid promiscuity were measured for the P. aeruginosa ortholog, not directly for KT2440 Q88P91.
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The report identifies no KT2440-specific experiment resolving net transfer direction or the outer-membrane docking partner.
Lipid-bound crystal structure of Pseudomonas putida Ttg2D