Evidence map›Paper›PMID 17586769›Full record

ArticleProtein science : a publication of the Protein Society2007

Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.

Darcie J Miller, Ludmilla Shuvalova, Elena Evdokimova, Alexei Savchenko, Alexander F Yakunin, Wayne F Anderson

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Activity and structure ofThe Journal of biological chemistry · 2019
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  13. Association between polymorphisms in the metallophosphoesterase (MPPE1) gene and bipolar disorder.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2010
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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

6 authors at 2 institutions in 2 countries.

Darcie J MillerDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA.
Ludmilla Shuvalova
Elena Evdokimova
Alexei Savchenko
Alexander F Yakunin
Wayne F Anderson
Northwestern University · USUniversity of Toronto · CA

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
DRUG DISCOVERY TRAINING IN AGE-RELATED DISORDERST32AG000260 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WATTERSON, DANIEL MARTIN · 1998 to 2010
$2.7M
NIA NIH HHS T32 AG000260NIA NIH HHS T32-AG00260NIGMS NIH HHS GM-62414NIGMS NIH HHS P50 GM062414
6 · The paper itself

Abstract

Escherichia coli YfcE belongs to a conserved protein family within the calcineurin-like phosphoesterase superfamily (Pfam00149) that is widely distributed in bacteria and archaea. Superfamily members are metallophosphatases that include monoesterases and diesterases involved in a variety of cellular functions. YfcE exhibited catalytic activity against bis-p-nitrophenyl phosphate, a general substrate for phosphodiesterases, and had an absolute requirement for Mn2+. However, no activity was observed with phosphodiesters and over 50 naturally occurring phosphomonoesters. The crystal structure of the YfcE phosphodiesterase has been determined to 2.25 A resolution. YfcE has a beta-sandwich architecture similar to metallophosphatases of common ancestral origin. Unlike its more complex homologs that have added structural elements for regulation and substrate recognition, the relatively small 184-amino-acid protein has retained its ancestral simplicity. The tetrameric protein carries two zinc ions per active site from the E. coli extract that reflect the conserved di-Mn2+ active site geometry. A cocrystallized sulfate inhibitor mimics the binding of phosphate moeities in known ligand/phosphatase complexes. Thus, YfcE has a similar active site and biochemical mechanism as well-characterized superfamily members, while the YfcE phosphodiester-containing substrate is unique.

Indexed as

Amino Acid SequenceCatalysisCrystallography, X-RayDeoxyribonucleasesDimerizationEscherichia coli ProteinsHydrolysisManganeseModels, MolecularMolecular Sequence DataPhosphatesPhosphoric Diester HydrolasesProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidStructural Homology, ProteinDeoxyribonucleasesEscherichia coli ProteinsManganesePhosphatesPhosphoric Diester HydrolasesSulfates

Identifiers

PMID17586769
PMCPMC2206680
OpenAlexW2119740343

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.