Evidence map›Paper›PMID 37935699›Full record

ArticleNature communications2023

Structural basis of peptide secretion for Quorum sensing by ComA.

Lin Yu, Xin Xu, Wan-Zhen Chua, Hao Feng, Zheng Ser, Kai Shao, Jian Shi, Yumei Wang, Zongli Li, Radoslaw M Sobota and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.8field-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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

12 authors at 4 institutions in 3 countries.

Lin Yu *Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Xin Xu *Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Wan-Zhen Chua *Infectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, 117545, Singapore.ORCID 0000-0001-9714-8463
Hao Feng *Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Zheng SerFunctional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.
Kai ShaoDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Jian ShiDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Yumei WangBeijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Science, Beijing, 100190, China.
Zongli LiHarvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA, 02115, USA.ORCID 0000-0002-1237-7556
Radoslaw M SobotaFunctional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore, 138673, Singapore.ORCID 0000-0002-2455-2526
Lok-To ShamInfectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, 117545, Singapore. lsham@nus.edu.sg.ORCID 0000-0001-9047-0310
Min LuoDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore. dbslmin@nus.edu.sg.ORCID 0000-0002-3493-2282
National University of Singapore · SGAgency for Science, Technology and Research · SGHarvard University · USInstitute of Physics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quorum sensing (QS) is a crucial regulatory mechanism controlling bacterial signalling and holds promise for novel therapies against antimicrobial resistance. In Gram-positive bacteria, such as Streptococcus pneumoniae, ComA is a conserved efflux pump responsible for the maturation and secretion of peptide signals, including the competence-stimulating peptide (CSP), yet its structure and function remain unclear. Here, we functionally characterize ComA as an ABC transporter with high ATP affinity and determined its cryo-EM structures in the presence or absence of CSP or nucleotides. Our findings reveal a network of strong electrostatic interactions unique to ComA at the intracellular gate, a putative binding pocket for two CSP molecules, and negatively charged residues facilitating CSP translocation. Mutations of these residues affect ComA's peptidase activity in-vitro and prevent CSP export in-vivo. We demonstrate that ATP-Mg

Indexed as

Bacterial ProteinsQuorum SensingAdenosine TriphosphatePeptidesStreptococcus pneumoniaeAdenosine TriphosphateBacterial ProteinsPeptides

Identifiers

PMID37935699
PMCPMC10630487
OpenAlexW4388451932

What OpenQuestion holds

Textmetadata
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.