Evidence map›Paper›PMID 23954504›Full record

ArticleStructure (London, England : 1993)2013

Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling.

Anna I Podgornaia, Patricia Casino, Alberto Marina, Michael T Laub

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Review
  2. Two-Component Systems inVeterinary sciences · 2025
    Review
  3. Article
  4. Article
  5. Novel Coumarins Derivatives for A. baumannii Lung Infection Developed by High-Throughput Screening and Reinforcement Learning.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2024
    Article
  6. Article
  7. A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023
    Article
  8. Marginal specificity in protein interactions constrains evolution of a paralogous family.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Exopolysaccharides metabolism and cariogenesis ofJournal of oral microbiology · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
  17. Article
  18. Article
  19. Article
  20. TheFrontiers in microbiology · 2018
    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

4 authors.

Anna I PodgornaiaComputational and Systems Biology Initiative, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Patricia Casino
Alberto Marina
Michael T Laub

Funding

Graduate Training in Computational and Systems BiologyT32GM087237 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BURGE, CHRISTOPHER B · 2009 to 2023
$4.6M
Cell Cycle Regulation in Caulobacter CrescentusR01GM082899 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUB, MICHAEL · 2008 to 2020
$3.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM082899NIGMS NIH HHS T32 GM087237
6 · The paper itself

Abstract

Two-component signal transduction systems typically involve a sensor histidine kinase that specifically phosphorylates a single, cognate response regulator. This protein-protein interaction relies on molecular recognition via a small set of residues in each protein. To better understand how these residues determine the specificity of kinase-substrate interactions, we rationally rewired the interaction interface of a Thermotoga maritima two-component system, HK853-RR468, to match that found in a different two-component system, Escherichia coli PhoR-PhoB. The rewired proteins interacted robustly with each other, but no longer interacted with the parent proteins. Analysis of the crystal structures of the wild-type and mutant protein complexes and a systematic mutagenesis study reveal how individual mutations contribute to the rewiring of interaction specificity. Our approach and conclusions have implications for studies of other protein-protein interactions and protein evolution and for the design of novel protein interfaces.

Indexed as

Amino Acid SubstitutionAmino Acid SequenceBacterial ProteinsCatalytic DomainCrystallography, X-RayEscherichia coliModels, MolecularProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, SecondarySequence Homology, Amino AcidSignal TransductionThermotoga maritimaBacterial ProteinsPhoB protein, BacteriaPhoR protein, Bacteria

Identifiers

PMID23954504
PMCPMC3821218

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.