Evidence map›Paper›PMID 23791943›Full record

ArticleStructure (London, England : 1993)2013

Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations.

D Sean Froese, Farhad Forouhar, Timothy H Tran, Melanie Vollmar, Yi Seul Kim, Scott Lew, Helen Neely, Jayaraman Seetharaman, Yang Shen, Rong Xiao and 18 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Heterogenous Clinical Landscape in a Consanguineous Malonic Aciduria Family.International journal of molecular sciences · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A Single Amino Acid Mutation Converts (The Journal of biological chemistry · 2017
    Article
  11. 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

28 authors at 4 institutions in 2 countries.

D Sean FroeseStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, UK.
Farhad Forouhar
Timothy H Tran
Melanie Vollmar
Yi Seul Kim
Scott Lew
Helen Neely
Jayaraman Seetharaman
Yang Shen
Rong Xiao
Thomas B Acton
John K Everett
Giuseppe Cannone
Sriharsha Puranik
Pavel Savitsky
Tobias Krojer
Ewa S Pilka
Wasim Kiyani
Wen Hwa Lee
Brian D Marsden
Frank von Delft
Charles K Allerston
Laura Spagnolo
Opher Gileadi
Gaetano T Montelione
Udo Oppermann
Wyatt W Yue
Liang Tong
University of Oxford · GBNew York Structural Biology Center · USRutgers, The State University of New Jersey · USUniversity of Edinburgh · GB

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI DETITTA, GEORGE T · 2010 to 2014
$36.9M
Structural biology of enzymes in fatty acid metabolismR01DK067238 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2004 to 2012
$2.6M
CIHRNIDDK NIH HHS R01 DK067238NIGMS NIH HHS U54 GM094597Wellcome Trust 087658Wellcome Trust 092809
6 · The paper itself

Abstract

Malonyl-coenzyme A decarboxylase (MCD) is found from bacteria to humans, has important roles in regulating fatty acid metabolism and food intake, and is an attractive target for drug discovery. We report here four crystal structures of MCD from human, Rhodopseudomonas palustris, Agrobacterium vitis, and Cupriavidus metallidurans at up to 2.3 Å resolution. The MCD monomer contains an N-terminal helical domain involved in oligomerization and a C-terminal catalytic domain. The four structures exhibit substantial differences in the organization of the helical domains and, consequently, the oligomeric states and intersubunit interfaces. Unexpectedly, the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis. Our structures, along with mutagenesis and kinetic studies, provide a molecular basis for understanding pathogenic mutations and catalysis, as well as a template for structure-based drug design.

Indexed as

Mutation, MissenseAmino Acid SequenceBacterial ProteinsCarboxy-LyasesCatalytic DomainCrystallography, X-RayDeficiency DiseasesEnzyme StabilityHumansHydrogen BondingKineticsModels, MolecularMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, SecondaryStructural Homology, ProteinBacterial ProteinsCarboxy-Lyasesmalonyl-CoA decarboxylase

Identifiers

PMID23791943
PMCPMC3701320
OpenAlexW2107440860

What OpenQuestion holds

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LicenceCC BY
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.