Evidence map›Paper›PMID 19346475›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Dissection of the high rate constant for the binding of a ribotoxin to the ribosome.

Sanbo Qin, Huan-Xiang Zhou

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Theoretical frameworks for multiscale modeling and simulation.Current opinion in structural biology · 2014
    Review
  5. Modeling protein association mechanisms and kinetics.Current opinion in structural biology · 2013
    Review
  6. Article
  7. PIBiophysical reviews · 2013
    Article
  8. Poisson-Boltzmann Calculations: van der Waals or Molecular Surface?Communications in computational physics · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Automated prediction of protein association rate constants.Structure (London, England : 1993) · 2011
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Rate theories for biologists.Quarterly reviews of biophysics · 2010
    Review
  19. Darwinian biophysics: electrostatics and evolution in the kinetics of molecular binding.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Sanbo QinDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
Huan-Xiang Zhou
Florida State University · US

Funding

THEORY OF PROTEIN/PROTEIN ASSOCIATIONR01GM058187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 1998 to 2016
$3.7M
NIGMS NIH HHS GM058187NIGMS NIH HHS R01 GM058187
6 · The paper itself

Abstract

Restrictocin belongs to a family of site-specific ribonucleases that kill cells by inactivating the ribosome. The restrictocin-ribosome binding rate constant was observed to exceed 10(10) M(-1) s(-1). We have developed a transient-complex theory to model the binding rates of protein-protein and protein-RNA complexes. The theory predicts the rate constant as k(a) = k(a0) exp(-DeltaG(el)*/k(B)T), where k(a0) is the basal rate constant for reaching the transient complex, located at the outer boundary of the bound state, by random diffusion, and DeltaG(el)* is the average electrostatic interaction free energy of the transient complex. Here, we applied the transient-complex theory to dissect the high restrictocin-ribosome binding rate constant. We found that the binding rate of restrictocin to the isolated sarcin/ricin loop is electrostatically enhanced by approximately 300-fold, similar to results found in other protein-protein and protein-RNA complexes. The ribosome provides an additional 10,000-fold rate enhancement because of two synergistic mechanisms afforded by the distal regions of the ribosome. First, they provide additional electrostatic attraction with restrictocin. Second, they reposition the transient complex into a region where local electrostatic interactions of restrictocin with the sarcin/ricin loop are particularly favorable. Our calculations rationalize a host of experimental observations and identify a strategy for designing proteins that bind their targets with high speed.

Indexed as

HalobacteriaceaeModels, MolecularMutationOsmolar ConcentrationProtein BindingProtein Structure, TertiaryRibonucleasesRibosomesStatic ElectricityRibonucleases

Identifiers

PMID19346475
PMCPMC2678469
OpenAlexW2159577634

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.