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Crystal structure of NucB, a biofilm-degrading endonuclease

DOI: 10.1093/nar/gkx1170 DOI Help

Authors: Arnaud Basle (Newcastle University) , Lorraine Hewitt (Newcastle University) , Alan Koh (Newcastle University) , Heather K. Lamb (Newcastle University) , Paul Thompson (Newcastle University) , J. Grant Burgess (Newcastle University) , Michael J. Hall (Newcastle University) , Alastair R. Hawkins (Newcastle University) , Heath Murray (Newcastle University) , Richard J. Lewis (Newcastle University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research

State: Published (Approved)
Published: November 2017
Diamond Proposal Number(s): 7864

Open Access Open Access

Abstract: Bacterial biofilms are a complex architecture of cells that grow on moist interfaces, and are held together by a molecular glue of extracellular proteins, sugars and nucleic acids. Biofilms are particularly problematic in human healthcare as they can coat medical implants and are thus a potential source of disease. The enzymatic dispersal of biofilms is increasingly being developed as a new strategy to treat this problem. Here, we have characterized NucB, a biofilm-dispersing nuclease from a marine strain of Bacillus licheniformis, and present its crystal structure together with the biochemistry and a mutational analysis required to confirm its active site. Taken together, these data support the categorization of NucB into a unique subfamily of the ββα metal-dependent non-specific endonucleases. Understanding the structure and function of NucB will facilitate its future development into an anti-biofilm therapeutic agent.

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography


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