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4YFU

Crystal structure of open Bacillus fragment DNA polymerase bound to DNA and dTTP

Summary for 4YFU
Entry DOI10.2210/pdb4yfu/pdb
Related PRD IDPRD_900003
DescriptorDNA polymerase, Primer DNA, Template DNA, ... (7 entities in total)
Functional Keywordsprotein-dna complex, transferase-dna complex, transferase/dna
Biological sourceGeobacillus stearothermophilus
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Total number of polymer chains6
Total formula weight147910.23
Authors
Wu, E.Y. (deposition date: 2015-02-25, release date: 2015-07-22, Last modification date: 2024-11-06)
Primary citationMiller, B.R.,Beese, L.S.,Parish, C.A.,Wu, E.Y.
The Closing Mechanism of DNA Polymerase I at Atomic Resolution.
Structure, 23:1609-1620, 2015
Cited by
PubMed Abstract: DNA 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.
PubMed: 26211612
DOI: 10.1016/j.str.2015.06.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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数据于2025-06-18公开中

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