6CFX
Bosea sp GapR solved in the presence of DNA
Summary for 6CFX
Entry DOI | 10.2210/pdb6cfx/pdb |
Descriptor | UPF0335 protein ASE63_04290, PHOSPHATE ION (3 entities in total) |
Functional Keywords | caulobacter, dna binding, nap, dna twist, dna binding protein |
Biological source | Bosea sp. Root381 |
Total number of polymer chains | 4 |
Total formula weight | 36374.69 |
Authors | Schumacher, M.A. (deposition date: 2018-02-18, release date: 2018-09-12, Last modification date: 2023-10-04) |
Primary citation | Guo, M.S.,Haakonsen, D.L.,Zeng, W.,Schumacher, M.A.,Laub, M.T. A Bacterial Chromosome Structuring Protein Binds Overtwisted DNA to Stimulate Type II Topoisomerases and Enable DNA Replication. Cell, 175:583-, 2018 Cited by PubMed Abstract: 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. PubMed: 30220456DOI: 10.1016/j.cell.2018.08.029 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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