2O4V

An arginine ladder in OprP mediates phosphate specific transfer across the outer membrane

Summary for 2O4V

Entry DOI	10.2210/pdb2o4v/pdb
Descriptor	Porin P, CALCIUM ION, PHOSPHATE ION, ... (7 entities in total)
Functional Keywords	outer membrane, porin, phosphate, transport, channel, membrane protein
Biological source	Pseudomonas aeruginosa PAO1
Cellular location	Cell outer membrane; Multi-pass membrane protein: P05695
Total number of polymer chains	3
Total formula weight	137689.39
Authors	Moraes, T.F.,Bains, M.,Hancock, R.E.,Strynadka, N.C. (deposition date: 2006-12-05, release date: 2006-12-26, Last modification date: 2023-12-27)
Primary citation	Moraes, T.F.,Bains, M.,Hancock, R.E.,Strynadka, N.C. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nat.Struct.Mol.Biol., 14:85-87, 2007 Cited by PubMed Abstract: 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-A 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. PubMed: 17187075 DOI: 10.1038/nsmb1189 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.94 Å)

Structure validation