3fyx

The Structure of OmpF porin with a synthetic dibenzo-18-crown-6 as modulator

spinqualitylabelsall models 3fyx, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fyx is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: 451, EPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OMPF_ECOLI Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2. 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 attachment of modulators to a trimeric porin ion channel was investigated (see picture of the trimer with a crown ether modulator (orange)). The interplay of modulator and protein is essential for the conformational heterogeneity of the hybrid channel. Single-site attachment in large pores is not sufficient to change the electrophysiological characteristics of the pores-such change requires additional noncovalent interactions or second-site attachments. On the function and structure of synthetically modified porins.,Reitz S, Cebi M, Reiss P, Studnik G, Linne U, Koert U, Essen LO Angew Chem Int Ed Engl. 2009;48(26):4853-7. PMID:19322865 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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