Evidence map›Paper›PMID 26211612›Full record

ArticleStructure (London, England : 1993)2015

The Closing Mechanism of DNA Polymerase I at Atomic Resolution.

Bill R Miller, Lorena S Beese, Carol A Parish, Eugene Y Wu

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. A four-point molecular handover during Okazaki maturation.Nature structural & molecular biology · 2023
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  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Bill R MillerDepartment of Biology, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA; Department of Chemistry, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA.
Lorena S BeeseDepartment of Biochemistry, Duke University Medical Center, 255 Nanaline H. Duke Building, Durham, NC 27710, USA.
Carol A ParishDepartment of Chemistry, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA. Electronic address: cparish@richmond.edu.
Eugene Y WuDepartment of Biology, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA; Department of Biochemistry, Duke University Medical Center, 255 Nanaline H. Duke Building, Durham, NC 27710, USA. Electronic address: ewu@richmond.edu.

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WALTER J. CHAZIN · 2001 to 2026
$89.6M
STRUCTURE AND MECHANISM OF PROTEIN PRENYLTRANSFERASESR01GM052382 · NIGMS · DUKE UNIVERSITY · PI BEESE, LORENA S · 1995 to 2002
$893k
Structural biology of human DNA mismatch repair machineryR01GM091487 · NIGMS · DUKE UNIVERSITY · PI BEESE, LORENA S. · 2009 to 2010
$647k
NCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM052382NIGMS NIH HHS R01 GM091487
6 · The paper itself

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.

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayDNA Polymerase IGeobacillus stearothermophilusHistidineModels, MolecularMolecular Dynamics SimulationNucleotidesProtein Structure, SecondaryBacterial ProteinsDNA Polymerase IHistidineNucleotides

Identifiers

PMID26211612
PMCPMC5036450

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.