Evidence map›Paper›PMID 25372812›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii.

Thomas A Bobik, Erick J Morales, Annie Shin, Duilio Cascio, Michael R Sawaya, Mark Arbing, Todd O Yeates, Madeline E Rasche

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
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

8 authors at 3 institutions in 1 country.

Thomas A BobikRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Erick J MoralesDepartment of Chemistry and Biochemistry, California State University, Fullerton, CA 92834, USA.
Annie ShinDepartment of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
Duilio CascioDepartment of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
Michael R SawayaDepartment of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
Mark ArbingDepartment of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
Todd O YeatesDepartment of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
Madeline E RascheDepartment of Chemistry and Biochemistry, California State University, Fullerton, CA 92834, USA.
University of California, Los Angeles · USCalifornia State University, Fullerton · USIowa State University · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
NCRR NIH HHS 5P41RR015301-10NCRR NIH HHS P41 RR015301NIGMS NIH HHS 8 P41 GM103403-10NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Prior studies have indicated that MJ1099 from Methanocaldococcus jannaschii has roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archaea. Here, the structure of MJ1099 has been solved to 1.7 Å resolution using anomalous scattering methods. The results indicate that MJ1099 is a member of the TIM-barrel superfamily and that it is a homohexamer. Bioinformatic analyses identified a potential active site that is highly conserved among MJ1099 homologs and the key amino acids involved were identified. The results presented here should guide further studies of MJ1099 including mechanistic studies and possibly the development of inhibitors that target the methanogenic archaea in the digestive tracts of humans and that are a source of the greenhouse gas methane.

Indexed as

Bacterial ProteinsBinding SitesCrystallographyFuransMethanocaldococcusProtein Structure, SecondaryProtein Structure, TertiaryPterinsRecombinant ProteinsBacterial Proteinscarbon dioxide reduction factorFuransmethanopterinPterinsRecombinant ProteinsMethanocaldococcus jannaschiimethanofuranmethanopterinMJ1099

Identifiers

PMID25372812
PMCPMC4231847
OpenAlexW2023891978

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.