Evidence map›Paper›PMID 24332718›Full record

ArticleStructure (London, England : 1993)2014

A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport.

Qin Yang, Sven Brüschweiler, James J Chou

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
  2. Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022
    Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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.

Qin YangDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Sven BrüschweilerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
James J ChouDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: chou@cmcd.hms.harvard.edu.

Funding

Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI SANDERS, CHARLES R · 2010 to 2014
$11.5M
AvanceIII 700MHz NMR spectrometer with cryogenic probeS10RR029236 · NCRR · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2010
$1.6M
NCRR NIH HHS S10 RR029236NIGMS NIH HHS GM094608NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

The mitochondrial carriers play essential roles in energy metabolism. The short Ca²⁺-binding mitochondrial carrier (SCaMC) transports ATP-Mg in exchange for Pi and is important for activities that depend on adenine nucleotides. SCaMC adopts, in addition to the transmembrane domain (TMD) that transports solutes, an extramembrane N-terminal domain (NTD) that regulates solute transport in a Ca²⁺-dependent manner. Crystal structure of the Ca²⁺-bound NTD reveals a compact architecture in which the functional EF hands are sequestered by an endogenous helical segment. Nuclear magnetic resonance (NMR) relaxation rates indicated that removal of Ca²⁺ from NTD results in a major conformational switch from the rigid and compact Ca²⁺-bound state to the dynamic and loose apo state. Finally, we showed using surface plasmon resonance and NMR titration experiments that free apo NTDs could specifically interact with liposome-incorporated TMD, but that Ca²⁺ binding drastically weakened the interaction. Our results together provide a molecular explanation for Ca²⁺-dependent ATP-Mg flux in mitochondria.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAntiportersCalciumCalcium-Binding ProteinsCalmodulinCrystallography, X-RayHumansMagnesiumMagnetic Resonance SpectroscopyMitochondriaMitochondrial ProteinsMolecular Sequence DataPeptidesPhosphatesProtein Structure, TertiaryAdenosine TriphosphateAntiportersCalciumCalcium-Binding ProteinsCalmodulinMagnesiumMitochondrial ProteinsPeptidesPhosphatesProteolipidsproteoliposomesSLC25A24 protein, human

Identifiers

PMID24332718
PMCPMC3946054

What OpenQuestion holds

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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.