3F2D
DNA Polymerase PolC from Geobacillus kaustophilus complex with DNA, dGTP, Mn and Zn
Summary for 3F2D
Entry DOI | 10.2210/pdb3f2d/pdb |
Related | 3F2B 3F2C |
Descriptor | 5'-D(*DCP*DAP*DGP*DTP*DGP*DAP*DGP*DAP*DCP*DGP*DGP*DGP*DCP*DAP*DAP*DCP*DC)-3', 5'-D(*DAP*DTP*DAP*DAP*DCP*DGP*DGP*DTP*DTP*DGP*DCP*DCP*DCP*DGP*DTP*DCP*DTP*DCP*DAP*DCP*DTP*DG)-3', GEOBACILLUS KAUSTOPHILUS DNA POLC, ... (8 entities in total) |
Functional Keywords | dna polymerase c, dna polymerase iii, ternary complex, protein-dna complex, replicative polymerase, gram-positive, transferase-dna complex, transferase/dna |
Biological source | Geobacillus kaustophilus More |
Cellular location | Cytoplasm : Q5L0J3 |
Total number of polymer chains | 3 |
Total formula weight | 130191.00 |
Authors | Davies, D.R.,Evans, R.J.,Bullard, J.M.,Christensen, J.,Green, L.S.,Guiles, J.W.,Ribble, W.K.,Janjic, N.,Jarvis, T.C. (deposition date: 2008-10-29, release date: 2009-01-20, Last modification date: 2023-09-06) |
Primary citation | Evans, R.J.,Davies, D.R.,Bullard, J.M.,Christensen, J.,Green, L.S.,Guiles, J.W.,Pata, J.D.,Ribble, W.K.,Janjic, N.,Jarvis, T.C. Structure of PolC reveals unique DNA binding and fidelity determinants. Proc.Natl.Acad.Sci.USA, 105:20695-20700, 2008 Cited by PubMed Abstract: PolC is the polymerase responsible for genome duplication in many Gram-positive bacteria and represents an attractive target for antibacterial development. We have determined the 2.4-A resolution crystal structure of Geobacillus kaustophilus PolC in a ternary complex with DNA and dGTP. The structure reveals nascent base pair interactions that lead to highly accurate nucleotide incorporation. A unique beta-strand motif in the PolC thumb domain contacts the minor groove, allowing replication errors to be sensed up to 8 nt upstream of the active site. PolC exhibits the potential for large-scale conformational flexibility, which could encompass the catalytic residues. The structure suggests a mechanism by which the active site can communicate with the rest of the replisome to trigger proofreading after nucleotide misincorporation, leading to an integrated model for controlling the dynamic switch between replicative and repair polymerases. This ternary complex of a cellular replicative polymerase affords insights into polymerase fidelity, evolution, and structural diversity. PubMed: 19106298DOI: 10.1073/pnas.0809989106 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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