2o4v | pdb_00002o4v

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

spinqualitylabelsall models 2o4v, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o4v is a 3 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.94Å Ligands: C8E, CA, CL, GOL, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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