3fyx
From Proteopedia
The Structure of OmpF porin with a synthetic dibenzo-18-crown-6 as modulator
Structural highlights
FunctionOMPF_ECOLI Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.[1] 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 PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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