Evidence map›Paper›PMID 22365602›Full record

ArticleChemistry & biology2012

Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains.

Jesse A Sundlov, Ce Shi, Daniel J Wilson, Courtney C Aldrich, Andrew M Gulick

Abstract read
In one paragraph

Article in Chemistry & biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
–field-weighted citation impact
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

83 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Targeting Siderophore Biosynthesis to Thwart Microbial Growth.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  17. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Jesse A SundlovHauptman-Woodward Institute and Department of Structural Biology, University at Buffalo, Buffalo, NY 14203 USA.
Ce Shi
Daniel J Wilson
Courtney C Aldrich
Andrew M Gulick

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Structures of Peptide Synthetases and Related EnzymesR01GM068440 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI GULICK, ANDREW M · 2004 to 2013
$3.1M
NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIGMS NIH HHS GM-068440NIGMS NIH HHS R01 GM068440
6 · The paper itself

Abstract

Nonribosomal peptide synthetases (NRPSs) are modular proteins that produce peptide antibiotics and siderophores. These enzymes act as catalytic assembly lines where substrates, covalently bound to integrated carrier domains, are delivered to adjacent catalytic domains. The carrier domains are initially loaded by adenylation domains, which use two distinct conformations to catalyze sequentially the adenylation of the substrate and the thioesterification of the pantetheine cofactor. We have used a mechanism-based inhibitor to determine the crystal structure of an engineered adenylation-carrier domain protein illustrating the intermolecular interaction between the adenylation and carrier domains. This structure enabled directed mutations to improve the interaction between nonnative partner proteins. Comparison with prior NRPS adenylation domain structures provides insights into the assembly line dynamics of these modular enzymes.

Indexed as

Computer SimulationCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydrolasesKineticsLigasesMutationPeptide SynthasesProtein Structure, TertiaryRecombinant Fusion ProteinsSubstrate Specificity2,3-dihydroxybenzoate-AMP ligase, E coliEscherichia coli ProteinsHydrolasesisochorismataseLigasesPeptide SynthasesRecombinant Fusion Proteins

Identifiers

PMID22365602
PMCPMC3292774

What OpenQuestion holds

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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.