3FYX

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

Summary for 3FYX

• Entry DOI: 10.2210/pdb3fyx/pdb
• Descriptor: Outer membrane protein F, N-(6,7,9,10,17,18,20,21-octahydrodibenzo[b,k][1,4,7,10,13,16]hexaoxacyclooctadecin-2-yl)acetamide, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: beta-barrel, ion-channel engineering, porin structure, synthetic ion-current modulator, crown ether, cell membrane, cell outer membrane, ion transport, membrane, phage recognition, porin, transmembrane, transport, transport protein
• Biological source: Escherichia coli K12
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P02931
• Total number of polymer chains: 1
• Total formula weight: 37743.97

Authors

Reitz, S.,Cebi, M.,Koert, U.,Essen, L.O. (deposition date: 2009-01-23, release date: 2009-06-30, Last modification date: 2024-11-20)

Primary citation

Reitz, S.,Cebi, M.,Reiss, P.,Studnik, G.,Linne, U.,Koert, U.,Essen, L.O.
On the function and structure of synthetically modified porins.
Angew.Chem.Int.Ed.Engl., 48:4853-4857, 2009

PubMed Abstract: 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.

PubMed: 19322865
DOI: 10.1002/anie.200900457

Experimental method

X-RAY DIFFRACTION (3.4 Å)