Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 1, Pages 85-87Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1189
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The outer membrane protein OprP mediates the transport of essential phosphate anions into the pathogenic bacterium Pseudomonas aeruginosa. Here we report the crystallographic structure of trimeric OprP at 1.9-angstrom resolution, revealing an unprecedented 9-residue arginine 'ladder' that spans from the extracellular surface down through a constriction zone where phosphate is coordinated. Lysine residues coat the inner periplasmic surface, creating an 'electropositive sink' that pulls the phosphates through the eyelet and into the cell.
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