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| | ==Bosea sp GapR solved in the presence of DNA== | | ==Bosea sp GapR solved in the presence of DNA== |
| - | <StructureSection load='6cfx' size='340' side='right' caption='[[6cfx]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='6cfx' size='340' side='right'caption='[[6cfx]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cfx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bosea_sp._root381 Bosea sp. root381]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CFX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cfx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bosea_sp._Root381 Bosea sp. Root381]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CFX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASE63_04290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1736524 Bosea sp. Root381])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6cfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfx OCA], [http://pdbe.org/6cfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cfx RCSB], [http://www.ebi.ac.uk/pdbsum/6cfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfx ProSAT]</span></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=6cfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfx OCA], [https://pdbe.org/6cfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cfx RCSB], [https://www.ebi.ac.uk/pdbsum/6cfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0Q9HY32_9HYPH A0A0Q9HY32_9HYPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bosea sp. root381]] | + | [[Category: Bosea sp. Root381]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Large Structures]] |
| - | [[Category: Caulobacter]] | + | [[Category: Schumacher MA]] |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna twist]]
| + | |
| - | [[Category: Nap]]
| + | |
| Structural highlights
Function
A0A0Q9HY32_9HYPH
Publication Abstract from PubMed
When DNA is unwound during replication, it becomes overtwisted and forms positive supercoils in front of the translocating DNA polymerase. Unless removed or dissipated, this superhelical tension can impede replication elongation. Topoisomerases, including gyrase and topoisomerase IV in bacteria, are required to relax positive supercoils ahead of DNA polymerase but may not be sufficient for replication. Here, we find that GapR, a chromosome structuring protein in Caulobacter crescentus, is required to complete DNA replication. GapR associates in vivo with positively supercoiled chromosomal DNA, and our biochemical and structural studies demonstrate that GapR forms a dimer-of-dimers that fully encircles overtwisted DNA. Further, we show that GapR stimulates gyrase and topo IV to relax positive supercoils, thereby enabling DNA replication. Analogous chromosome structuring proteins that locate to the overtwisted DNA in front of replication forks may be present in other organisms, similarly helping to recruit and stimulate topoisomerases during DNA replication.
A Bacterial Chromosome Structuring Protein Binds Overtwisted DNA to Stimulate Type II Topoisomerases and Enable DNA Replication.,Guo MS, Haakonsen DL, Zeng W, Schumacher MA, Laub MT Cell. 2018 Sep 7. pii: S0092-8674(18)31045-6. doi: 10.1016/j.cell.2018.08.029. PMID:30220456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo MS, Haakonsen DL, Zeng W, Schumacher MA, Laub MT. A Bacterial Chromosome Structuring Protein Binds Overtwisted DNA to Stimulate Type II Topoisomerases and Enable DNA Replication. Cell. 2018 Sep 7. pii: S0092-8674(18)31045-6. doi: 10.1016/j.cell.2018.08.029. PMID:30220456 doi:http://dx.doi.org/10.1016/j.cell.2018.08.029
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