Evidence map›Paper›PMID 25693966›Full record

ArticleMicrobiologyOpen2015

Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII-like signal transduction protein.

Philip H Choi, Kamakshi Sureka, Joshua J Woodward, Liang Tong

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 50 citations in OpenAlex.

  1. A c-di-AMP-controlled glutamine synthesis pathway promotes persistence ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The role ofJournal of bacteriology · 2024
    Article
  7. Article
  8. Article
  9. Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  10. Bacterial aggregation facilitates internalin-mediated invasion ofFrontiers in cellular and infection microbiology · 2024
    Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020
    Review
  16. Review
  17. c-di-AMP assists osmoadaptation by regulating theThe Journal of biological chemistry · 2019
    Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Philip H ChoiDepartment of Biological Sciences, Columbia University, New York City, New York, 10027.
Kamakshi SurekaDepartment of Microbiology, University of Washington, Seattle, Washington, 98195.
Joshua J WoodwardDepartment of Microbiology, University of Washington, Seattle, Washington, 98195.
Liang TongDepartment of Biological Sciences, Columbia University, New York City, New York, 10027.
Columbia University · USUniversity of Washington · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007367 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI REINER, STEVEN L · 1985 to 2021
$25.1M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Listeria monocytogenes physiology and host pathogen interactionsR01AI116669 · NIAID · UNIVERSITY OF WASHINGTON · PI WOODWARD, JOSHUA · 2015 to 2024
$4.4M
Structural biology of enzymes in fatty acid metabolismR01DK067238 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2004 to 2012
$2.6M
Replacement of an aging X-ray diffraction system for protein crystallographyS10OD012018 · OD · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2012 to 2012
$405k
C-di-AMP signaling in Listeria monocytogenes host pathogen interactionsR56AI108698 · NIAID · UNIVERSITY OF WASHINGTON · PI WOODWARD, JOSHUA · 2014 to 2014
$341k
NIAID NIH HHS R01 AI116669NIAID NIH HHS R56 AI108698NIAID NIH HHS R56AI108698NIBIB NIH HHS P30 EB009998NIDDK NIH HHS R01 DK067238NIDDK NIH HHS R01DK067238NIGMS NIH HHS GM007367NIGMS NIH HHS T32 GM007367NIH HHS S10 OD012018NIH HHS S10OD012018
6 · The paper itself

Abstract

Cyclic-di-AMP (c-di-AMP) is a broadly conserved bacterial second messenger that is of importance in bacterial physiology. The molecular receptors mediating the cellular responses to the c-di-AMP signal are just beginning to be discovered. PstA is a previously uncharacterized PII -like protein which has been identified as a c-di-AMP receptor. PstA is widely distributed and conserved among Gram-positive bacteria in the phylum Firmicutes. Here, we report the biochemical, structural, and functional characterization of PstA from Listeria monocytogenes. We have determined the crystal structures of PstA in the c-di-AMP-bound and apo forms at 1.6 and 2.9 Å resolution, respectively, which provide the molecular basis for its specific recognition of c-di-AMP. PstA forms a homotrimer structure that has overall similarity to the PII protein family which binds ATP. However, PstA is markedly different from PII proteins in the loop regions, and these structural differences mediate the specific recognition of their respective nucleotide ligand. The residues composing the c-di-AMP binding pocket are conserved, suggesting that c-di-AMP recognition by PstA is of functional importance. Disruption of pstA in L. monocytogenes affected c-di-AMP-mediated alterations in bacterial growth and lysis. Overall, we have defined the PstA family as a conserved and specific c-di-AMP receptor in bacteria.

Indexed as

Signal TransductionAmino Acid SequenceATP-Binding Cassette TransportersBacterial ProteinsCarrier ProteinsConserved SequenceDinucleoside PhosphatesHumansHydrogen BondingListeria monocytogenesModels, MolecularMolecular Sequence DataMutationProtein BindingProtein ConformationSequence AlignmentATP-Binding Cassette TransportersBacterial ProteinsCarrier Proteinscyclic diadenosine phosphateDinucleoside Phosphatesphosphate-specific transport protein A, bacteriaCrystal structurecyclic-di-AMPFirmicutesListeria monocytogenesPII-like proteinsignal transduction

Identifiers

PMID25693966
PMCPMC4475381
OpenAlexW2129582162

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.