7 8 9 3 3 7
Home About us MoEF Contact us Sitemap Tamil Website  
About Envis
Whats New
Microorganisms
Research on Microbes
Database
Bibliography
Publications
Library
E-Resources
Microbiology Experts
Events
Online Submission
Access Statistics

Site Visitors

blog tracking


 
Journal of Structural Biology
Volume 204 (3), 2018, Pages 396-405

Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens

Amy E.Mc Grath, Alexander P.Martyn, Louise R.Whittell, Fay E.Dawes, Jennifer L.Beck, Nicholas E.Dixon, Michael J.Kelso, Aaron J.Oakley

Molecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, New South Wales, Australia.

Abstract

Bacterial sliding clamps bind to DNA and act as protein-protein interaction hubs for several proteins involved in DNA replication and repair. The partner proteins all bind to a common pocket on sliding clamps via conserved linear peptide sequence motifs, which suggest the pocket as an attractive target for development of new antibiotics. Herein we report the X-ray crystal structures and biochemical characterization of β sliding clamps from the Gram-negative pathogens Pseudomonas aeruginosaAcinetobacter baumannii and Enterobacter cloacae. The structures reveal close similarity between the pathogen and Escherichia coli clamps and similar patterns of binding to linear clamp-binding motif peptides. The results suggest that linear motif-sliding clamp interactions are well conserved and an antibiotic targeting the sliding clamp should have broad-spectrum activity against Gram-negative pathogens.

Graphical abstract

Keywords: Antimicrobials, ESKAPE pathogens, Sliding clamp.

Copyright © 2005 ENVIS Centre ! All rights reserved
This site is optimized for 1024 x 768 screen resolution