4cwe: Difference between revisions
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==Structural studies of rolling circle replication initiation protein from Staphylococcus aureus== | ==Structural studies of rolling circle replication initiation protein from Staphylococcus aureus== | ||
<StructureSection load='4cwe' size='340' side='right' caption='[[4cwe]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4cwe' size='340' side='right'caption='[[4cwe]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cwe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CWE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4cwe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CWE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cwe OCA], [https://pdbe.org/4cwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cwe RCSB], [https://www.ebi.ac.uk/pdbsum/4cwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cwe ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [https://www.uniprot.org/uniprot/REPN_STAAU REPN_STAAU] This protein is probably a specific topoisomerase involved in initiating replication. This protein is specifically required and may be rate-limiting for replication of the plasmid in vivo.[https://www.uniprot.org/uniprot/REPD_STAAU REPD_STAAU] This protein is probably a specific topoisomerase involved in initiating replication. This protein is specifically required and may be rate-limiting for replication of the plasmid in vivo. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Structures of replication initiation proteins from staphylococcal antibiotic resistance plasmids reveal protein asymmetry and flexibility are necessary for replication.,Carr SB, Phillips SE, Thomas CD Nucleic Acids Res. 2016 Jan 20. pii: gkv1539. PMID:26792891<ref>PMID:26792891</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cwe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Carr SB]] | ||
[[Category: | [[Category: Phillips SEV]] | ||
[[Category: | [[Category: Thomas CD]] | ||
Latest revision as of 15:17, 20 December 2023
Structural studies of rolling circle replication initiation protein from Staphylococcus aureusStructural studies of rolling circle replication initiation protein from Staphylococcus aureus
Structural highlights
FunctionREPN_STAAU This protein is probably a specific topoisomerase involved in initiating replication. This protein is specifically required and may be rate-limiting for replication of the plasmid in vivo.REPD_STAAU This protein is probably a specific topoisomerase involved in initiating replication. This protein is specifically required and may be rate-limiting for replication of the plasmid in vivo. Publication Abstract from PubMedAntibiotic 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. Structures of replication initiation proteins from staphylococcal antibiotic resistance plasmids reveal protein asymmetry and flexibility are necessary for replication.,Carr SB, Phillips SE, Thomas CD Nucleic Acids Res. 2016 Jan 20. pii: gkv1539. PMID:26792891[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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