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Crystal structure of open Bacillus fragment DNA polymerase bound to DNA and dTTPCrystal structure of open Bacillus fragment DNA polymerase bound to DNA and dTTP
Structural highlights
Publication Abstract from PubMedDNA polymerases must quickly and accurately distinguish between similar nucleic acids to form Watson-Crick base pairs and avoid DNA replication errors. Deoxynucleoside triphosphate (dNTP) binding to the DNA polymerase active site induces a large conformational change that is difficult to characterize experimentally on an atomic level. Here, we report an X-ray crystal structure of DNA polymerase I bound to DNA in the open conformation with a dNTP present in the active site. We use this structure to computationally simulate the open to closed transition of DNA polymerase in the presence of a Watson-Crick base pair. Our microsecond simulations allowed us to characterize the key steps involved in active site assembly, and propose the sequence of events involved in the prechemistry steps of DNA polymerase catalysis. They also reveal new features of the polymerase mechanism, such as a conserved histidine as a potential proton acceptor from the primer 3'-hydroxyl. The Closing Mechanism of DNA Polymerase I at Atomic Resolution.,Miller BR 3rd, Beese LS, Parish CA, Wu EY Structure. 2015 Jul 21. pii: S0969-2126(15)00269-5. doi:, 10.1016/j.str.2015.06.016. PMID:26211612[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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