PDBsum entry 6ehc

Membrane protein

PDB id: 6ehc

Contents

Protein chains

307 a.a.

Ligands

C8E ×10

Waters ×256

PDB id:

6ehc

Name:

Membrane protein

Title:

Ompudeltan (n-terminus deletion mutant of ompu), outer membrane protein of vibrio cholerae

Structure:

Outer membrane protein u. Chain: a, b. Synonym: porin ompu. Engineered: yes. Other_details: this is a n-terminal deletion mutant (first 10 resdiues deleted) of ompu (om porin) of vibrio cholerae.

Source:

Vibrio cholerae serotype o1 (strain atcc 39541 / classical ogawa 395 / o395). Organism_taxid: 345073. Strain: atcc 39541 / classical ogawa 395 / o395. Gene: ompu, vc0395_a0162, vc395_0650. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.02Å R-factor: 0.195 R-free: 0.248

Authors:

B.Van Den Berg,M.Pathania

Key ref:

M.Pathania et al. (2018). Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae. Structure, 26, 708. PubMed id: 29657131 DOI: 10.1016/j.str.2018.03.010

Date:

13-Sep-17 Release date: 25-Apr-18

Protein chains

A5F934  (OMPU_VIBC3) -  Outer membrane protein U from Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)

Seq: 341 a.a.

Struc: 307 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2018.03.010

Structure 26:708 (2018)

PubMed id: 29657131

Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae.

M.Pathania, S.Acosta-Gutierrez, S.P.Bhamidimarri, A.Baslé, M.Winterhalter, M.Ceccarelli, B.van den Berg.

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.