6ENE

OmpF orthologue from Enterobacter cloacae (OmpE35)

Summary for 6ENE

• Entry DOI: 10.2210/pdb6ene/pdb
• Descriptor: Outer membrane protein (Porin), SULFATE ION, octyl beta-D-glucopyranoside, ... (5 entities in total)
• Functional Keywords: porine ompf-orthologue, outer membrane, transport protein
• Biological source: Enterobacter cloacae
• Total number of polymer chains: 3
• Total formula weight: 111677.35

Authors

van den Berg, B.,Abellon-Ruiz, J.,Basle, A. (deposition date: 2017-10-04, release date: 2018-10-31, Last modification date: 2024-01-17)

Primary citation

Acosta-Gutierrez, S.,Ferrara, L.,Pathania, M.,Masi, M.,Wang, J.,Bodrenko, I.,Zahn, M.,Winterhalter, M.,Stavenger, R.A.,Pages, J.M.,Naismith, J.H.,van den Berg, B.,Page, M.G.P.,Ceccarelli, M.
Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins.
Acs Infect Dis., 4:1487-1498, 2018

PubMed Abstract: Small, hydrophilic molecules, including most important antibiotics in clinical use, cross the Gram-negative outer membrane through the water-filled channels provided by porins. We have determined the X-ray crystal structures of the principal general porins from three species of Enterobacteriaceae, namely Enterobacter aerogenes, Enterobacter cloacae, and Klebsiella pneumoniae, and determined their antibiotic permeabilities as well as those of the orthologues from Escherichia coli. Starting from the structure of the porins and molecules, we propose a physical mechanism underlying transport and condense it in a computationally efficient scoring function. The scoring function shows good agreement with in vitro penetration data and will enable the screening of virtual databases to identify molecules with optimal permeability through porins and help to guide the optimization of antibiotics with poor permeation.

PubMed: 29962203
DOI: 10.1021/acsinfecdis.8b00108

Experimental method

X-RAY DIFFRACTION (2.3 Å)