6EHC

OmpUdeltaN (N-terminus deletion mutant of OmpU), outer membrane protein of Vibrio cholerae

Summary for 6EHC

• Entry DOI: 10.2210/pdb6ehc/pdb
• Descriptor: Outer membrane protein U, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• Functional Keywords: outer membrane protein, porin, ompf or ompc ortholog, ion-transport, membrane beta barrel, ion-channel, membrane protein, diffusion porin, diffusion channel, non-specific porin.
• Biological source: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
• Cellular location: Cell outer membrane; Multi-pass membrane protein: A5F934
• Total number of polymer chains: 2
• Total formula weight: 70349.33

Authors

van den berg, B.,Pathania, M. (deposition date: 2017-09-13, release date: 2018-04-25, Last modification date: 2024-01-17)

Primary citation

Pathania, M.,Acosta-Gutierrez, S.,Bhamidimarri, S.P.,Basle, A.,Winterhalter, M.,Ceccarelli, M.,van den Berg, B.
Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae.
Structure, 26:708-721.e4, 2018

PubMed Abstract: The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecific, large-diameter channels for the diffusional uptake of small molecules required for cell growth and function. While the porins of Enterobacteriaceae (e.g., E. coli OmpF and OmpC) have been extensively characterized structurally and biochemically, much less is known about their counterparts in Vibrionaceae. Vibrio cholerae, the causative agent of cholera, has two major porins, OmpU and OmpT, for which no structural information is available despite their importance for the bacterium. Here we report high-resolution X-ray crystal structures of V. cholerae OmpU and OmpT complemented with molecular dynamics simulations. While similar overall to other general porins, the channels of OmpU and OmpT have unusual constrictions that create narrower barriers for small-molecule permeation and change the internal electric fields of the channels. Together with electrophysiological and in vitro transport data, our results illuminate small-molecule uptake within the Vibrionaceae.

PubMed: 29657131
DOI: 10.1016/j.str.2018.03.010

Experimental method

X-RAY DIFFRACTION (2.02 Å)