Evidence map›Paper›PMID 22925578›Full record

ArticleJournal of molecular biology2012

Characterization of transport proteins for aromatic compounds derived from lignin: benzoate derivative binding proteins.

Karolina Michalska, Changsoo Chang, Jamey C Mack, Sarah Zerbs, Andrzej Joachimiak, Frank R Collart

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Proteogenomic Characterization ofMicroorganisms · 2024
    Article
  6. Article
  7. Article
  8. Comparative Proteomics ofMicroorganisms · 2020
    Article
  9. Passive membrane transport of lignin-related compounds.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Transport capabilities of environmental Pseudomonads for sulfur compounds.Protein science : a publication of the Protein Society · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Modeling themSystems
    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.

Karolina MichalskaBiosciences Division, Argonne National Laboratory, 9700 South Cass Avenue, Lemont, IL 60439, USA.
Changsoo Chang
Jamey C Mack
Sarah Zerbs
Andrzej Joachimiak
Frank R Collart
Argonne National Laboratory · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM094585NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

In vitro growth experiments have demonstrated that aromatic compounds derived from lignin can be metabolized and represent a major carbon resource for many soil bacteria. However, the proteins that mediate the movement of these metabolites across the cell membrane have not been thoroughly characterized. To address this deficiency, we used a library representative of lignin degradation products and a thermal stability screen to determine ligand specificity for a set of solute-binding proteins (SBPs) from ATP-binding cassette (ABC) transporters. The ligand mapping process identified a set of proteins from Alphaproteobacteria that recognize various benzoate derivatives. Seven high-resolution crystal structures of these proteins in complex with four different aromatic compounds were obtained. The protein-ligand complexes provide details of molecular recognition that can be used to infer binding specificity. This structure-function characterization provides new insight for the biological roles of these ABC transporters and their SBPs, which had been previously annotated as branched-chain amino-acid-binding proteins. The knowledge derived from the crystal structures provides a foundation for development of sequence-based methods to predict the ligand specificity of other uncharacterized transporters. These results also demonstrate that Alphaproteobacteria possess a diverse set of transport capabilities for lignin-derived compounds. Characterization of this new class of transporters improves genomic annotation projects and provides insight into the metabolic potential of soil bacteria.

Indexed as

Biological Transport, ActiveAlphaproteobacteriaATP-Binding Cassette TransportersBacterial ProteinsBenzoatesBinding SitesCell MembraneCrystallography, X-RayLigandsLigninProtein BindingProtein FoldingProtein Structure, TertiaryStructure-Activity RelationshipATP-Binding Cassette TransportersBacterial ProteinsBenzoatesLigandsLignin

Identifiers

PMID22925578
PMCPMC3836681
OpenAlexW2000527772

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.