4pqk: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqk RCSB], [http://www.ebi.ac.uk/pdbsum/4pqk PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqk RCSB], [http://www.ebi.ac.uk/pdbsum/4pqk PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The staphylococcal multiresistance plasmids are key contributors to the alarming rise in bacterial multidrug resistance. A conserved replication initiator, RepA, encoded on these plasmids is essential for their propagation. RepA proteins consist of flexibly linked N-terminal (NTD) and C-terminal (CTD) domains. Despite their essential role in replication, the molecular basis for RepA function is unknown. Here we describe a complete structural and functional dissection of RepA proteins. Unexpectedly, both the RepA NTD and CTD show similarity to the corresponding domains of the bacterial primosome protein, DnaD. Although the RepA and DnaD NTD both contain winged helix-turn-helices, the DnaD NTD self-assembles into large scaffolds whereas the tetrameric RepA NTD binds DNA iterons using a newly described DNA binding mode. Strikingly, structural and atomic force microscopy data reveal that the NTD tetramer mediates DNA bridging, suggesting a molecular mechanism for origin handcuffing. Finally, data show that the RepA CTD interacts with the host DnaG primase, which binds the replicative helicase. Thus, these combined data reveal the molecular mechanism by which RepA mediates the specific replicon assembly of staphylococcal multiresistant plasmids. | |||
Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein.,Schumacher MA, Tonthat NK, Kwong SM, Chinnam NB, Liu MA, Skurray RA, Firth N Proc Natl Acad Sci U S A. 2014 Jun 9. pii: 201406065. PMID:24927575<ref>PMID:24927575</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:45, 23 July 2014
C-Terminal domain of DNA binding proteinC-Terminal domain of DNA binding protein
Structural highlights
Publication Abstract from PubMedThe staphylococcal multiresistance plasmids are key contributors to the alarming rise in bacterial multidrug resistance. A conserved replication initiator, RepA, encoded on these plasmids is essential for their propagation. RepA proteins consist of flexibly linked N-terminal (NTD) and C-terminal (CTD) domains. Despite their essential role in replication, the molecular basis for RepA function is unknown. Here we describe a complete structural and functional dissection of RepA proteins. Unexpectedly, both the RepA NTD and CTD show similarity to the corresponding domains of the bacterial primosome protein, DnaD. Although the RepA and DnaD NTD both contain winged helix-turn-helices, the DnaD NTD self-assembles into large scaffolds whereas the tetrameric RepA NTD binds DNA iterons using a newly described DNA binding mode. Strikingly, structural and atomic force microscopy data reveal that the NTD tetramer mediates DNA bridging, suggesting a molecular mechanism for origin handcuffing. Finally, data show that the RepA CTD interacts with the host DnaG primase, which binds the replicative helicase. Thus, these combined data reveal the molecular mechanism by which RepA mediates the specific replicon assembly of staphylococcal multiresistant plasmids. Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein.,Schumacher MA, Tonthat NK, Kwong SM, Chinnam NB, Liu MA, Skurray RA, Firth N Proc Natl Acad Sci U S A. 2014 Jun 9. pii: 201406065. PMID:24927575[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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