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| | <StructureSection load='4pt7' size='340' side='right'caption='[[4pt7]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='4pt7' size='340' side='right'caption='[[4pt7]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pt7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_ca-347 Staphylococcus aureus ca-347]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PT7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PT7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pt7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_CA-347 Staphylococcus aureus CA-347]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PT7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pta|4pta]], [[4pql|4pql]], [[4pqk|4pqk]]</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=4pt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pt7 OCA], [https://pdbe.org/4pt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pt7 RCSB], [https://www.ebi.ac.uk/pdbsum/4pt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pt7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA347_2788, repA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1323661 Staphylococcus aureus CA-347])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pt7 OCA], [http://pdbe.org/4pt7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pt7 RCSB], [http://www.ebi.ac.uk/pdbsum/4pt7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pt7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Staphylococcus aureus ca-347]] | + | [[Category: Staphylococcus aureus CA-347]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Schumacher MA]] |
| - | [[Category: Multidrug resistance]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Replication initiation]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schumacher MA, Tonthat NK, Kwong SM, Chinnam NB, Liu MA, Skurray RA, Firth N. Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein. Proc Natl Acad Sci U S A. 2014 Jun 9. pii: 201406065. PMID:24927575 doi:http://dx.doi.org/10.1073/pnas.1406065111
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