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-Å 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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We thank C. Egli and N. Martin for valuable discussion and the staff at the Advanced Light Source beamline 8.2.2 for data collection time and assistance. T.F.M. is supported by a Michael Smith Foundation for Health Research (MSFHR) postdoctoral fellowship. N.C.J.S. thanks the Howard Hughes International Scholar program and the Canadian Institutes of Health Research (CIHR) for funding and the Canadian Foundation for Innovation and the MSFHR for infrastructure support. R.E.W.H. thanks the CIHR for funding, the Canadian Cystic Fibrosis Foundation and the US Cystic Fibrosis Foundation. N.C.J.S. is a MSFHR Senior Scholar, CIHR Investigator and Howard Hughes Medical Institute International Scholar. R.E.W.H. is a CIHR Investigator.
The authors declare no competing financial interests.
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