Evidence map›Paper›PMID 19520856›Full record

ArticleThe Journal of biological chemistry2009

Substrate-induced conformational changes in the essential peripheral membrane-associated mannosyltransferase PimA from mycobacteria: implications for catalysis.

Marcelo E Guerin, Francis Schaeffer, Alain Chaffotte, Petra Gest, David Giganti, Jana Korduláková, Mark van der Woerd, Mary Jackson, Pedro M Alzari

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Functional and mechanistic characterization of the phosphatidyl-Frontiers in cellular and infection microbiology · 2026
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  9. The Phosphatidyl-Journal of bacteriology · 2021
    Article
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  11. Group A, B, C, and GThe Journal of biological chemistry · 2019
    Article
  12. Article
  13. Spatially distinct and metabolically active membrane domain in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
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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

9 authors at 6 institutions in 4 countries.

Marcelo E GuerinDepartment of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, Colorado 80523-1682, USA. mrcguerin@gmail.com
Francis Schaeffer
Alain Chaffotte
Petra Gest
David Giganti
Jana Korduláková
Mark van der Woerd
Mary Jackson
Pedro M Alzari
Bipar · FRCentre de Biologie Structurale · FRColorado State University · USCentre National de la Recherche Scientifique · FRComenius University Bratislava · SKInstitut Pasteur · FR

Funding

Biogenesis of Lipoarabinomannan in MycobacteriaR01AI064798 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI JACKSON, MARY · 2005 to 2019
$5.4M
NIAID NIH HHS AI064798NIAID NIH HHS R01 AI064798
6 · The paper itself

Abstract

Phosphatidyl-myo-inositol mannosyltransferase A (PimA) is an essential glycosyltransferase (GT) involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), which are key components of the mycobacterial cell envelope. PimA is the paradigm of a large family of peripheral membrane-binding GTs for which the molecular mechanism of substrate/membrane recognition and catalysis is still unknown. Strong evidence is provided showing that PimA undergoes significant conformational changes upon substrate binding. Specifically, the binding of the donor GDP-Man triggered an important interdomain rearrangement that stabilized the enzyme and generated the binding site for the acceptor substrate, phosphatidyl-myo-inositol (PI). The interaction of PimA with the beta-phosphate of GDP-Man was essential for this conformational change to occur. In contrast, binding of PI had the opposite effect, inducing the formation of a more relaxed complex with PimA. Interestingly, GDP-Man stabilized and PI destabilized PimA by a similar enthalpic amount, suggesting that they formed or disrupted an equivalent number of interactions within the PimA complexes. Furthermore, molecular docking and site-directed mutagenesis experiments provided novel insights into the architecture of the myo-inositol 1-phosphate binding site and the involvement of an essential amphiphatic alpha-helix in membrane binding. Altogether, our experimental data support a model wherein the flexibility and conformational transitions confer the adaptability of PimA to the donor and acceptor substrates, which seems to be of importance during catalysis. The proposed mechanism has implications for the comprehension of the peripheral membrane-binding GTs at the molecular level.

Indexed as

Bacterial ProteinsCalorimetryCatalysisCell MembraneCircular DichroismGuanosine DiphosphateMannosyltransferasesModels, BiologicalModels, ChemicalMolecular ConformationMycobacterium smegmatisProtein DenaturationProtein Structure, TertiarySubstrate SpecificityThermodynamicsBacterial ProteinsGuanosine DiphosphateMannosyltransferasesphosphatidyl-myo-inositol mannosyltransferase PimA, Mycobacterium smegmatis

Identifiers

PMID19520856
PMCPMC2755885
OpenAlexW2010208000

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.