Evidence map›Paper›PMID 24748621›Full record

ArticleThe Journal of biological chemistry2014

Allostery and conformational dynamics in cAMP-binding acyltransferases.

Marjetka Podobnik, Nida Siddiqui, Katja Rebolj, Subhalaxmi Nambi, Franci Merzel, Sandhya S Visweswariah

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. A universal stress protein inThe Journal of biological chemistry · 2020
    Article
  3. Article
  4. Insect ArylalkylamineFrontiers in molecular biosciences · 2018
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. A universal stress protein (USP) in mycobacteria binds cAMP.The Journal of biological chemistry · 2015
    Article
  10. 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

6 authors at 1 institution in 1 country.

Marjetka PodobnikFrom the Laboratory for Molecular Biology and Nanobiotechnology and marjetka.podobnik@ki.si.
Nida SiddiquiDepartment of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.
Katja ReboljFrom the Laboratory for Molecular Biology and Nanobiotechnology and.
Subhalaxmi NambiDepartment of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.
Franci MerzelLaboratory of Biomolecular Structure, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia and.
Sandhya S VisweswariahDepartment of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India sandhya@mrdg.iisc.ernet.in.
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacteria harbor unique proteins that regulate protein lysine acylation in a cAMP-regulated manner. These lysine acyltransferases from Mycobacterium smegmatis (KATms) and Mycobacterium tuberculosis (KATmt) show distinctive biochemical properties in terms of cAMP binding affinity to the N-terminal cyclic nucleotide binding domain and allosteric activation of the C-terminal acyltransferase domain. Here we provide evidence for structural features in KATms that account for high affinity cAMP binding and elevated acyltransferase activity in the absence of cAMP. Structure-guided mutational analysis converted KATms from a cAMP-regulated to a cAMP-dependent acyltransferase and identified a unique asparagine residue in the acyltransferase domain of KATms that assists in the enzymatic reaction in the absence of a highly conserved glutamate residue seen in Gcn5-related N-acetyltransferase-like acyltransferases. Thus, we have identified mechanisms by which properties of similar proteins have diverged in two species of mycobacteria by modifications in amino acid sequence, which can dramatically alter the abundance of conformational states adopted by a protein.

Indexed as

AcyltransferasesAllosteric RegulationCyclic AMPModels, MolecularMycobacteriumProtein BindingProtein ConformationAcyltransferasesCyclic AMPAcyltransferaseAllosteric RegulationCrystal StructureCyclic AMP (cAMP)Molecular DynamicsMycobacteriaProtein Acylation

Identifiers

PMID24748621
PMCPMC4047424
OpenAlexW2049488728

What OpenQuestion holds

Textmetadata
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.