Evidence map›Paper›PMID 19026779›Full record

ArticleMolecular cell2008

The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.

Agnidipta Ghosh, Stewart Shuman, Christopher D Lima

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 86 citations in OpenAlex.

  1. Trial
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  3. TheInternational journal of molecular sciences · 2025
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  19. Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016
    Review
  20. 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 1 institution in 1 country.

Agnidipta GhoshStructural Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
Stewart Shuman
Christopher D Lima
Kettering University · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
STRUCTURAL STUDIES OF THE MRNA CAPPING APPARATUSR01GM061906 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI LIMA, CHRISTOPHER D. · 2000 to 2013
$4.8M
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS GM52470NIGMS NIH HHS GM61906NIGMS NIH HHS R01 GM052470NIGMS NIH HHS R01 GM061906
6 · The paper itself

Abstract

Kinases and phosphatases regulate mRNA synthesis and processing by phosphorylating and dephosphorylating the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. Fcp1 is an essential CTD phosphatase that preferentially hydrolyzes Ser2-PO(4) of the tandem YSPTSPS CTD heptad array. Fcp1 crystal structures were captured at two stages of the reaction pathway: a Mg-BeF(3) complex that mimics the aspartylphosphate intermediate and a Mg-AlF(4)(-) complex that mimics the transition state of the hydrolysis step. Fcp1 is a Y-shaped protein composed of an acylphosphatase domain located at the base of a deep canyon formed by flanking modules that are missing from the small CTD phosphatase (SCP) clade: an Fcp1-specific helical domain and a C-terminal BRCA1 C-terminal (BRCT) domain. The structure and mutational analysis reveals that Fcp1 and Scp1 (a Ser5-selective phosphatase) adopt different CTD-binding modes; we surmise the CTD threads through the Fcp1 canyon to access the active site.

Indexed as

Amino Acid SequenceBinding SitesConsensus SequenceCrystallography, X-RayHydrogen BondingHydrolysisModels, MolecularMolecular Sequence DataMutation, MissensePhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRepetitive Sequences, Amino AcidRNA Polymerase IIcarboxy-terminal domain phosphatasePhosphoprotein PhosphatasesRNA Polymerase II

Identifiers

PMID19026779
PMCPMC2645342
OpenAlexW2071337049

What OpenQuestion holds

Textmetadata
LicenceTDM
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.