4CWE
Structural studies of rolling circle replication initiation protein from Staphylococcus aureus
Summary for 4CWE
Entry DOI | 10.2210/pdb4cwe/pdb |
Related | 4CWC |
Descriptor | REPLICATION INITIATION PROTEIN, REPLICATION INITIATION PROTEIN (1 entity in total) |
Functional Keywords | isomerase, antibiotic resistance, pcra helicase, dna relaxase, chimera |
Biological source | STAPHYLOCOCCUS AUREUS |
Total number of polymer chains | 2 |
Total formula weight | 68472.21 |
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 citation | Carr, 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: 26792891DOI: 10.1093/NAR/GKV1539 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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