6hms | pdb_00006hms

Cryo-EM map of DNA polymerase D from Pyrococcus abyssi in complex with DNA

Loading... Status: waiting for Mol* initialization Structural highlights 6hms is a 4 chain structure with sequence from "pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, ZN Gene: polB, PYRAB01210, PAB2266 ("Pyrococcus abyssi" Erauso et al. 1993), polC, PYRAB01200, PAB2404 ("Pyrococcus abyssi" Erauso et al. 1993) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DP2S_PYRAB] Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity). [DP2L_PYRAB] Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity). Publication Abstract from PubMed PolD is an archaeal replicative DNA polymerase (DNAP) made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2). Recently, we reported the individual crystal structures of the DP1 and DP2 catalytic cores, thereby revealing that PolD is an atypical DNAP that has all functional properties of a replicative DNAP but with the catalytic core of an RNA polymerase (RNAP). We now report the DNA-bound cryo-electron microscopy (cryo-EM) structure of the heterodimeric DP1-DP2 PolD complex from Pyrococcus abyssi, revealing a unique DNA-binding site. Comparison of PolD and RNAPs extends their structural similarities and brings to light the minimal catalytic core shared by all cellular transcriptases. Finally, elucidating the structure of the PolD DP1-DP2 interface, which is conserved in all eukaryotic replicative DNAPs, clarifies their evolutionary relationships with PolD and sheds light on the domain acquisition and exchange mechanism that occurred during the evolution of the eukaryotic replisome. Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.,Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brule S, Beguin P, Henneke G, Lindahl E, Delarue M, Sauguet L PLoS Biol. 2019 Jan 18;17(1):e3000122. doi: 10.1371/journal.pbio.3000122. PMID:30657780 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA polymerase 3D structures

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