Structure of New Binary and Ternary DNA Polymerase Complexes From Bacteriophage RB69

• DOI: 10.3389/fmolb.2021.704813
• Publication Date: 2021-11-18T09:36:14Z
• Authors: Jongseo Park; Hyung-Seop Youn; Jun Yop An; Youngjin Lee; Soo Hyun Eom; Jimin Wang
• Keywords: Ternary complex; Divalent; Primer (cosmetics); Klenow fragment

DNA polymerase plays a critical role in passing the genetic information of any living organism to its offspring. from enterobacteria phage RB69 (RB69pol) has both polymerization and exonuclease activities been extensively studied as model system for B-family polymerases. Many binary ternary complex structures RB69pol are known, they all contain single polymerase-primer/template (P/T) complex. Here, we report crystal structure exonuclease-deficient with P/T duplex dimeric form at resolution 2.2 Å. The includes one new closed divalent metal ion bound open pre-insertion state vacant dNTP-binding pocket. These complexes suggest that initial binding correct dNTP is much weaker than expected second also measured. Additional conformational changes required convert these high-affinity states. Thus, measured affinities incoming ions average values many conformationally distinctive Our provides insights into order assembly involving two ions. biological relevance specific interactions observed between within this discussed.