Evidence map›Paper›PMID 22019591›Full record

ArticleJournal of molecular biology2011

Structure of the Escherichia coli phosphonate binding protein PhnD and rationally optimized phosphonate biosensors.

Ismael Alicea, Jonathan S Marvin, Aleksandr E Miklos, Andrew D Ellington, Loren L Looger, Eric R Schreiter

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Structural basis and evolutionary pathways of glycerol-1-phosphate transport in marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Lipid Trafficking in Diverse Bacteria.Accounts of chemical research · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Structural dynamics in the evolution of a bilobed protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Review
  14. Spontaneous Phage Resistance in Avian PathogenicFrontiers in microbiology · 2021
    Article
  15. Analytical chemistry · 2020
    Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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.

Ismael AliceaDepartment of Chemistry, University of Puerto Rico, Río Piedras, San Juan, Puerto Rico 00931.
Jonathan S Marvin
Aleksandr E Miklos
Andrew D Ellington
Loren L Looger
Eric R Schreiter

Funding

Upgrade Laboratories Facilities at UPR-Rio PiedrasR25GM061151 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI CARBALLEIRA, NESTOR MANUEL · 2001 to 2023
$32.5M
Structural Contexts and Functional Consequences of Protein S-nitrosylationSC1GM084852 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI SCHREITER, ERIC R · 2009 to 2010
$632k
Howard Hughes Medical InstituteNCI NIH HHS Y1-CO-1020NIGMS NIH HHS R25 GM061151NIGMS NIH HHS R25GM61151NIGMS NIH HHS SC1 GM084852NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The phnD gene of Escherichia coli encodes the periplasmic binding protein of the phosphonate (Pn) uptake and utilization pathway. We have crystallized and determined structures of E. coli PhnD (EcPhnD) in the absence of ligand and in complex with the environmentally abundant 2-aminoethylphosphonate (2AEP). Similar to other bacterial periplasmic binding proteins, 2AEP binds near the center of mass of EcPhnD in a cleft formed between two lobes. Comparison of the open, unliganded structure with the closed 2AEP-bound structure shows that the two lobes pivot around a hinge by ~70° between the two states. Extensive hydrogen bonding and electrostatic interactions stabilize 2AEP, which binds to EcPhnD with low nanomolar affinity. These structures provide insight into Pn uptake by bacteria and facilitated the rational design of high signal-to-noise Pn biosensors based on both coupled small-molecule dyes and autocatalytic fluorescent proteins.

Indexed as

Biosensing TechniquesCalorimetryCarrier ProteinsCatalysisColoring AgentsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFluorescent DyesModels, MolecularMolecular ConformationOrganophosphonatesOrganophosphorus CompoundsProtein Binding(2-(dimethylamino)ethyl)phosphonic acidCarrier ProteinsColoring AgentsEscherichia coli ProteinsFluorescent DyesOrganophosphonatesOrganophosphorus CompoundsPhnD protein, E coli

Identifiers

PMID22019591
PMCPMC5320564

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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.