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2W82

The structure of ArdA

Summary for 2W82
Entry DOI10.2210/pdb2w82/pdb
DescriptorORF18 (2 entities in total)
Functional Keywordsdna mimic, replication inhibitor
Biological sourceENTEROCOCCUS FAECALIS
Total number of polymer chains4
Total formula weight76543.53
Authors
McMahon, S.A.,Roberts, G.A.,Carter, L.G.,Cooper, L.P.,Liu, H.,White, J.H.,Johnson, K.A.,Sanghvi, B.,Oke, M.,Walkinshaw, M.D.,Blakely, G.,Naismith, J.H.,Dryden, D.T.F. (deposition date: 2009-01-08, release date: 2009-01-27, Last modification date: 2024-05-08)
Primary citationMcmahon, S.A.,Roberts, G.A.,Johnson, K.A.,Cooper, L.P.,Liu, H.,White, J.H.,Carter, L.G.,Sanghvi, B.,Oke, M.,Walkinshaw, M.D.,Blakely, G.,Naismith, J.H.,Dryden, D.T.F.
Extensive DNA Mimicry by the Arda Anti-Restriction Protein and its Role in the Spread of Antibiotic Resistance.
Nucleic Acids Res., 37:4887-, 2009
Cited by
PubMed Abstract: The ardA gene, found in many prokaryotes including important pathogenic species, allows associated mobile genetic elements to evade the ubiquitous Type I DNA restriction systems and thereby assist the spread of resistance genes in bacterial populations. As such, ardA contributes to a major healthcare problem. We have solved the structure of the ArdA protein from the conjugative transposon Tn916 and find that it has a novel extremely elongated curved cylindrical structure with defined helical grooves. The high density of aspartate and glutamate residues on the surface follow a helical pattern and the whole protein mimics a 42-base pair stretch of B-form DNA making ArdA by far the largest DNA mimic known. Each monomer of this dimeric structure comprises three alpha-beta domains, each with a different fold. These domains have the same fold as previously determined proteins possessing entirely different functions. This DNA mimicry explains how ArdA can bind and inhibit the Type I restriction enzymes and we demonstrate that 6 different ardA from pathogenic bacteria can function in Escherichia coli hosting a range of different Type I restriction systems.
PubMed: 19506028
DOI: 10.1093/NAR/GKP478
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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