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] Publication Abstract from PubMedOmpF, a multiionic porin from Escherichia coli, is a useful protypical model system for addressing general questions about electrostatic interactions in the confinement of an aqueous molecular pore. Here, anion binding sites in the OmpF pore were mapped by anomalous X-ray scattering of Br- ions from four different crystal structures and compared with Mg2+ sites and Rb+ sites from a previous anomalous diffraction study to provide a complete picture of cation and anion transfer paths along the OmpF channel. By comparing structures with various crystallization conditions, we find that anions bind in discrete clusters along the entire length of the OmpF pore, whereas cations find conserved binding sites with the extracellular, surface-exposed loops. Results from molecular dynamics simulations are consistent with the experimental data and help highlight the critical residues that preferentially contact either cations or anions during permeation. Analysis of these results provides new insights into the molecular mechanisms that determine ion selectivity in OmpF porin. A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations.,Dhakshnamoorthy B, Ziervogel BK, Blachowicz L, Roux B J Am Chem Soc. 2013 Oct 9. PMID:24106986[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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