Evidence map›Paper›PMID 18362338›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

X-ray crystal structure of the polymerase domain of the bacteriophage N4 virion RNA polymerase.

Katsuhiko S Murakami, Elena K Davydova, Lucia B Rothman-Denes

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.6field-weighted citation impact, top 8% of its field
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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Viral Genome Delivery Across Bacterial Cell Surfaces.Annual review of microbiology · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Novel N4 Bacteriophages Prevail in the Cold Biosphere.Applied and environmental microbiology · 2015
    Article
  13. Review
  14. Review
  15. X-ray crystal structures elucidate the nucleotidyl transfer reaction of transcript initiation using two nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. Article
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

3 authors at 2 institutions in 1 country.

Katsuhiko S MurakamiDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. kum14@psu.edu
Elena K Davydova
Lucia B Rothman-Denes
University of Chicago · USPennsylvania State University · US

Funding

Transcribing Activities in N4 Infected E. ColiR01AI012575 · NIAID · UNIVERSITY OF CHICAGO · PI ROTHMAN-DENES, LUCIA B. B · 1985 to 2013
$7.0M
X-RAY CRYSTALLOGRAPHIC STUDIES OF TAQ RNA POLYMERASER01GM061898 · NIGMS · ROCKEFELLER UNIVERSITY · PI DARST, SETH A. · 2000 to 2008
$3.3M
X-Ray Crystallographic Studies of N4 RNA PolymerasesR01GM071897 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI MURAKAMI, KATSUHIKO · 2004 to 2008
$1.1M
NIAID NIH HHS AI12575NIAID NIH HHS R01 AI012575NIGMS NIH HHS GM071897NIGMS NIH HHS GM61898NIGMS NIH HHS R01 GM061898NIGMS NIH HHS R01 GM071897
6 · The paper itself

Abstract

Coliphage N4 virion RNA polymerase (vRNAP), which is injected into the host upon infection, transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure. Here, we describe the 2.0-A resolution x-ray crystal structure of N4 mini-vRNAP, a member of the T7-like, single-unit RNAP family and the minimal component having all RNAP functions of the full-length vRNAP. The structure resembles a "fisted right hand" with Fingers, Palm and Thumb subdomains connected to an N-terminal domain. We established that the specificity loop extending from the Fingers along with W129 of the N-terminal domain play critical roles in hairpin-promoter recognition. A comparison with the structure of the T7 RNAP initiation complex reveals that the pathway of the DNA to the active site is blocked in the apo-form vRNAP, indicating that vRNAP must undergo a large-scale conformational change upon promoter DNA binding and explaining the highly restricted promoter specificity of vRNAP that is essential for phage early transcription.

Indexed as

Bacteriophage N4Crystallography, X-RayDNADNA-Directed RNA PolymerasesModels, MolecularPromoter Regions, GeneticProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryVirionDNADNA-Directed RNA Polymerases

Identifiers

PMID18362338
PMCPMC2278199
OpenAlexW2011800673

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.