Evidence map›Paper›PMID 24704788›Full record

ArticleNature structural & molecular biology2014

Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.

Jacob L W Morgan, Joshua T McNamara, Jochen Zimmer

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 172 papers.

0numbers the graph read from it
0cells of the map it votes in
172citing papers in PubMed
14.1field-weighted citation impact, top 1% 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

172 citing papers in PubMed, 352 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. A molecular description of plant cellulose biosynthesis inhibition.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

112 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Jacob L W MorganCenter for Membrane Biology, Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Joshua T McNamaraCenter for Membrane Biology, Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Jochen ZimmerCenter for Membrane Biology, Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
University of Virginia · US

Funding

Mechanism of Cellulose Synthesis and Transport Across Biological MembranesR01GM101001 · NIGMS · UNIVERSITY OF VIRGINIA · PI ZIMMER, JOCHEN · 2012 to 2021
$3.7M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS R01 GM101001NIGMS NIH HHS R01GM101001NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The bacterial signaling molecule cyclic di-GMP (c-di-GMP) stimulates the synthesis of bacterial cellulose, which is frequently found in biofilms. Bacterial cellulose is synthesized and translocated across the inner membrane by a complex of cellulose synthase BcsA and BcsB subunits. Here we present crystal structures of the c-di-GMP-activated BcsA-BcsB complex. The structures reveal that c-di-GMP releases an autoinhibited state of the enzyme by breaking a salt bridge that otherwise tethers a conserved gating loop that controls access to and substrate coordination at the active site. Disrupting the salt bridge by mutagenesis generates a constitutively active cellulose synthase. Additionally, the c-di-GMP-activated BcsA-BcsB complex contains a nascent cellulose polymer whose terminal glucose unit rests at a new location above BcsA's active site and is positioned for catalysis. Our mechanistic insights indicate how c-di-GMP allosterically modulates enzymatic functions.

Indexed as

Bacterial ProteinsBinding SitesCelluloseCrystallography, X-RayCyclic GMPGlucosyltransferasesModels, MolecularProtein Structure, TertiaryRhodobacter sphaeroidesBacterial ProteinsCellulosecellulose synthaseCyclic GMPGlucosyltransferases

Identifiers

PMID24704788
PMCPMC4013215
OpenAlexW2037365513

What OpenQuestion holds

Textmetadata
LicenceTDM
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.