Cation selective pathway of OmpF porin revealed by anomalous X-ray diffraction

The OmpF porin from the Escherichia coli outer membrane folds into a trimer of β-barrel, each forming a wide aqueous pore allowing the passage of ions and small solutes. A long loop (L3) carrying multiple acidic residues folds into the β-barrel pore to form a narrow “constriction zone”. A strong and...

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Bibliografiske detaljer
Main Authors: Dhakshnamoorthy, Balasundaresan, Raychaudhury, Suchismita, Blachowicz, Lydia, Roux, Benoît
Format: Artigo
Sprog:Inglês
Udgivet: 2009
Fag:
Article
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3584447/
https://ncbi.nlm.nih.gov/pubmed/19932117
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2009.11.042
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