Evidence map›Paper›PMID 25675500›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Visualization of a radical B12 enzyme with its G-protein chaperone.

Marco Jost, Valentin Cracan, Paul A Hubbard, Ruma Banerjee, Catherine L Drennan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
1.5field-weighted citation impact, top 18% 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, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Redox-Linked Coordination Chemistry Directs Vitamin BAccounts of chemical research · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A New Facet of Vitamin BAnnual review of biochemistry · 2017
    Review
  12. Review
  13. Vitamin BCurrent opinion in chemical biology · 2017
    Review
  14. Article
  15. Article
  16. 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

5 authors at 2 institutions in 1 country.

Marco JostDepartment of Chemistry and.
Valentin CracanDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0600.
Paul A HubbardDepartment of Chemistry and.
Ruma BanerjeeDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0600.
Catherine L DrennanDepartment of Chemistry and Department of Biology, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139; and cdrennan@mit.edu.
University of Michigan–Ann Arbor · USMassachusetts Institute of Technology · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
REACTION MECHANISMS OF MAMMALIAN B12-DEPENDENT ENZYMESR01DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI RUMA V BANERJEE · 1998 to 2026
$9.7M
Complex Metallocluster Structure and AssemblyR01GM069857 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2004 to 2017
$3.1M
REACTION MECHANISMS OF COBALAMIN-DEPENDENT ENZYMESR29DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1993 to 1997
–
NIDDK NIH HHS DK45776NIDDK NIH HHS R01 DK045776NIGMS NIH HHS GM069857NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM069857
6 · The paper itself

Abstract

G-protein metallochaperones ensure fidelity during cofactor assembly for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and biofuel development applications. Here, we present crystal structures of IcmF, a natural fusion protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein chaperone, which reveal the molecular architecture of a G-protein metallochaperone in complex with its target protein. These structures show that conserved G-protein elements become ordered upon target protein association, creating the molecular pathways that both sense and report on the cofactor loading state. Structures determined of both apo- and holo-forms of IcmF depict both open and closed enzyme states, in which the cofactor-binding domain is alternatively positioned for cofactor loading and for catalysis. Notably, the G protein moves as a unit with the cofactor-binding domain, providing a visualization of how a chaperone assists in the sequestering of a precious cofactor inside an enzyme active site.

Indexed as

ApoproteinsCatalytic DomainCoenzymesConserved SequenceCrystallography, X-RayCupriavidusGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine DiphosphateMethylmalonyl-CoA MutaseMitochondrial Membrane Transport ProteinsModels, MolecularMolecular ChaperonesProtein BindingProtein Structure, TertiaryProtein SubunitsApoproteinsCoenzymesGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine DiphosphateMethylmalonyl-CoA MutaseMitochondrial Membrane Transport ProteinsMolecular ChaperonesProtein SubunitscrystallographyG proteinmetallochaperonemetallocofactor deliveryvitamin B12

Identifiers

PMID25675500
PMCPMC4345561
OpenAlexW2157507482

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.