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4CWE

Structural studies of rolling circle replication initiation protein from Staphylococcus aureus

Summary for 4CWE
Entry DOI10.2210/pdb4cwe/pdb
Related4CWC
DescriptorREPLICATION INITIATION PROTEIN, REPLICATION INITIATION PROTEIN (1 entity in total)
Functional Keywordsisomerase, antibiotic resistance, pcra helicase, dna relaxase, chimera
Biological sourceSTAPHYLOCOCCUS AUREUS
Total number of polymer chains2
Total formula weight68472.21
Authors
Carr, S.B.,Phillips, S.E.V.,Thomas, C.D. (deposition date: 2014-04-02, release date: 2015-04-15, Last modification date: 2023-12-20)
Primary citationCarr, S.B.,Phillips, S.E.,Thomas, C.D.
Structures of Replication Initiation Proteins from Staphylococcal Antibiotic Resistance Plasmids Reveal Protein Asymmetry and Flexibility are Necessary for Replication.
Nucleic Acids Res., 44:2417-, 2016
Cited by
PubMed Abstract: Antibiotic resistance in pathogenic bacteria is a continual threat to human health, often residing in extrachromosomal plasmid DNA. Plasmids of the pT181 family are widespread and confer various antibiotic resistances to Staphylococcus aureus. They replicate via a rolling circle mechanism that requires a multi-functional, plasmid-encoded replication protein to initiate replication, recruit a helicase to the site of initiation and terminate replication after DNA synthesis is complete. We present the first atomic resolution structures of three such replication proteins that reveal distinct, functionally relevant conformations. The proteins possess a unique active site and have been shown to contain a catalytically essential metal ion that is bound in a manner distinct from that of any other rolling circle replication proteins. These structures are the first examples of the Rep_trans Pfam family providing insights into the replication of numerous antibiotic resistance plasmids from Gram-positive bacteria, Gram-negative phage and the mobilisation of DNA by conjugative transposons.
PubMed: 26792891
DOI: 10.1093/NAR/GKV1539
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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