3f2b

DNA Polymerase PolC from Geobacillus kaustophilus complex with DNA, dGTP, Mg and Zn

spinqualitylabelsall models 3f2b, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f2b is a 3 chain structure with sequence from "bacillus_kaustophilus"_prickett_1928 "bacillus kaustophilus" prickett 1928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DGT, MG, PO4, ZN Related: 3f2c, 3f2d Gene: GK1258, polC ("Bacillus kaustophilus" Prickett 1928) Activity: DNA-directed DNA polymerase, with EC number 2.7.7.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q5L0J3_GEOKA] Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity (By similarity).[HAMAP-Rule:MF_00356][SAAS:SAAS029460_004_008054] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of PolC reveals unique DNA binding and fidelity determinants.,Evans RJ, Davies DR, Bullard JM, Christensen J, Green LS, Guiles JW, Pata JD, Ribble WK, Janjic N, Jarvis TC Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20695-700. Epub 2008 Dec 23. PMID:19106298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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