Structural highlights
Function
[PORP_PSEAE] Anion specific, the binding site has higher affinity for phosphate than chloride ions. Porin O has a higher affinity for polyphosphates (tripolyphosphate and pyrophosphate) while porin P has a higher affinity for orthophosphate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane.,Moraes TF, Bains M, Hancock RE, Strynadka NC Nat Struct Mol Biol. 2007 Jan;14(1):85-7. Epub 2006 Dec 24. PMID:17187075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moraes TF, Bains M, Hancock RE, Strynadka NC. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nat Struct Mol Biol. 2007 Jan;14(1):85-7. Epub 2006 Dec 24. PMID:17187075 doi:10.1038/nsmb1189
