Structural highlights
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.[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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Duval V, Nicoloff H, Levy SB. Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli. Antimicrob Agents Chemother. 2009 Nov;53(11):4944-8. doi: 10.1128/AAC.00787-09., Epub 2009 Aug 31. PMID:19721064 doi:10.1128/AAC.00787-09
- ↑ Reitz S, Cebi M, Reiss P, Studnik G, Linne U, Koert U, Essen LO. On the function and structure of synthetically modified porins. Angew Chem Int Ed Engl. 2009;48(26):4853-7. PMID:19322865 doi:10.1002/anie.200900457
