Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae, one such pump comprises the inner membrane proton antiporter VceB, the periplasmic adaptor VceA, and the outer membrane channel VceC. Here, we report the crystal structure of VceC at 1.8 A resolution. The trimeric VceC is organized in the crystal lattice within laminar arrays that resemble membranes. A well resolved detergent molecule within this array interacts with the transmembrane beta-barrel domain in a fashion that may mimic protein-lipopolysaccharide contacts. Our analyses of the external surfaces of VceC and other channel proteins suggest that different classes of efflux pumps have distinct architectures. We discuss the implications of these findings for mechanisms of drug and protein export.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1074/jbc.M500401200 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Generative design of crystal structures by point cloud representations and diffusion model.
iScience
January 2025
School of Physics and Electronic Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.
Efficiently generating energetically stable crystal structures has long been a challenge in material design, primarily due to the immense arrangement of atoms in a crystal lattice. To facilitate the discovery of stable materials, we present a framework for the generation of synthesizable materials leveraging a point cloud representation to encode intricate structural information. At the heart of this framework lies the introduction of a diffusion model as its foundational pillar.
View Article and Find Full Text PDFAn easy-to-use three-dimensional protein-structure-prediction online platform "DPL3D" based on deep learning algorithms.
Curr Res Struct Biol
June 2025
The College of Health Humanities, Jinzhou Medical University, Jinzhou, 121001, China.
The change in the three-dimensional (3D) structure of a protein can affect its own function or interaction with other protein(s), which may lead to disease(s). Gene mutations, especially missense mutations, are the main cause of changes in protein structure. Due to the lack of protein crystal structure data, about three-quarters of human mutant proteins cannot be predicted or accurately predicted, and the pathogenicity of missense mutations can only be indirectly evaluated by evolutionary conservation.
View Article and Find Full Text PDFNovel D-Ribofuranosyl Tetrazoles: Synthesis, Characterization, In Vitro Antimicrobial Activity, and Computational Studies.
ACS Omega
January 2025
Applied Chemistry and Environment Laboratory, Applied Bioorganic Chemistry Team, Faculty of Science, Ibn Zohr University, Agadir 80000, Morocco.
The goal of this study was to synthesize and evaluate new antimicrobial compounds. We specifically focused on the development of 2,5-disubstituted tetrazole derivatives containing the O-methyl-2,3-O-isopropylidene-(D)-ribofuranoside groups through N-alkylation reactions. The synthesized compounds were characterized using H and C nuclear magnetic resonance (NMR) spectroscopy.
View Article and Find Full Text PDFNegative linear compressibility and structural stability of the energetic material -hexanitrostilbene under pressure.
Phys Chem Chem Phys
January 2025
School of Materials and Energy, University of Electronic Science and Technology of China, Chengdu 611731, Sichuan, China.
The structural stability of the energetic material 2,2',4,4',6,6'-hexanitrostilbene (-HNS) under high pressure is critical for optimizing its detonation performance and low sensitivity. However, its structural response to external pressure has not been sufficiently investigated. In this study, high-pressure single-crystal X-ray diffraction data of -HNS demonstrate that the sample exhibits pronounced anisotropic strain, demonstrating an unusual negative linear compressibility (NLC) along the axis, with a coefficient of -4.
View Article and Find Full Text PDFAn isolable boron-centered radical anion stabilized by a carbazole moiety.
Dalton Trans
January 2025
Hebei Center for New Inorganic Optoelectronic Nanomaterial Research, Hebei Key Laboratory of Heterocyclic Compounds, College of Chemical Engineering and Materials, Handan University, Handan 056002, P. R. China.
The isolation of a stable persistent carbazole-stabilized boron-centered monoradical anion 1˙, which has a high spin density at the B atom, has been reported. It is characterized using the crystal structure and UV-vis absorption spectrum, as well as electron paramagnetic resonance spectroscopy. Interestingly, the B-N bond was activated by the boron-centered radical anion 1˙, which had not been reported before.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!