4rjw | pdb_00004rjw

Crystal structure of Pseudomonas aeruginosa OprO

spinqualitylabelsall models 4rjw, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rjw is a 1 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. Ligands: C8E Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PORO_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. Publication Abstract from PubMed The outer membrane (OM) of Gram-negative bacteria functions as a selective permeability barrier between cell and environment. For nutrient acquisition, the OM contains a number of channels that mediate uptake of small molecules by diffusion. Many of these channels are specific, i.e., they prefer certain substrates over others. In electrophysiological experiments, the OM channels OprP and OprO from Pseudomonas aeruginosa show a specificity for phosphate and diphosphate, respectively. In this study we use x-ray crystallography, free-energy molecular dynamics (MD) simulations, and electrophysiology to uncover the atomic basis for the different substrate specificity of these highly similar channels. A structural analysis of OprP and OprO revealed two crucial differences in the central constriction region. In OprP there are two tyrosine residues, Y62 and Y114, whereas the corresponding residues in OprO are phenylalanine F62 and aspartate D114. To probe the importance of these two residues in generating the different substrate specificities, the double mutants were generated in silico and in vitro. Applied-field MD simulations and electrophysiological experiments demonstrated that the double mutations interchange the phosphate and diphosphate specificities of OprP and OprO. Our findings outline a possible strategy to rationally design channel specificity by modification of a small number of residues that may be applicable to other pores as well. Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa.,Modi N, Ganguly S, Barcena-Uribarri I, Benz R, van den Berg B, Kleinekathofer U Biophys J. 2015 Oct 6;109(7):1429-38. doi: 10.1016/j.bpj.2015.07.035. PMID:26445443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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