- PDB-8eil: C-Terminal Domain of BrxL from Acinetobacter BREX type I phage re... -
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Basic information
Entry
Database: PDB / ID: 8eil
Title
C-Terminal Domain of BrxL from Acinetobacter BREX type I phage restriction system
Components
Protease Lon-related BREX system protein BrxL
Keywords
DNA BINDING PROTEIN / helicase / phage restriction / LonP/RadA homolog / BREX
Function / homology
Function and homology information
ATP-dependent peptidase activity / protein catabolic process / serine-type endopeptidase activity / proteolysis / ATP binding Similarity search - Function
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1R15GM140375-01A1
United States
Citation
Journal: Nucleic Acids Res / Year: 2023 Title: Structure, substrate binding and activity of a unique AAA+ protein: the BrxL phage restriction factor. Authors: Betty W Shen / Lindsey A Doyle / Rachel Werther / Abigail A Westburg / Daniel P Bies / Stephanie I Walter / Yvette A Luyten / Richard D Morgan / Barry L Stoddard / Brett K Kaiser / Abstract: Bacteriophage exclusion ('BREX') systems are multi-protein complexes encoded by a variety of bacteria and archaea that restrict phage by an unknown mechanism. One BREX factor, termed BrxL, has been ...Bacteriophage exclusion ('BREX') systems are multi-protein complexes encoded by a variety of bacteria and archaea that restrict phage by an unknown mechanism. One BREX factor, termed BrxL, has been noted to display sequence similarity to various AAA+ protein factors including Lon protease. In this study we describe multiple CryoEM structures of BrxL that demonstrate it to be a chambered, ATP-dependent DNA binding protein. The largest BrxL assemblage corresponds to a dimer of heptamers in the absence of bound DNA, versus a dimer of hexamers when DNA is bound in its central pore. The protein displays DNA-dependent ATPase activity, and ATP binding promotes assembly of the complex on DNA. Point mutations within several regions of the protein-DNA complex alter one or more in vitro behaviors and activities, including ATPase activity and ATP-dependent association with DNA. However, only the disruption of the ATPase active site fully eliminates phage restriction, indicating that other mutations can still complement BrxL function within the context of an otherwise intact BREX system. BrxL displays significant structural homology to MCM subunits (the replicative helicase in archaea and eukaryotes), implying that it and other BREX factors may collaborate to disrupt initiation of phage DNA replication.
A: Protease Lon-related BREX system protein BrxL B: Protease Lon-related BREX system protein BrxL C: Protease Lon-related BREX system protein BrxL D: Protease Lon-related BREX system protein BrxL hetero molecules
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