Evidence map›Paper›PMID 12297624›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.

D M Himmel, S Gourinath, L Reshetnikova, Y Shen, A G Szent-Györgyi, C Cohen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Article
  2. Article
  3. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. ADisease models & mechanisms · 2017
    Article
  14. Article
  15. Article
  16. Highly selective inhibition of myosin motors provides the basis of potential therapeutic application.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Article
  19. Article
  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.

D M HimmelRosenstiel Basic Medical Sciences Research Center, Waltham, MA 02454-9110, USA.
S Gourinath
L Reshetnikova
Y Shen
A G Szent-Györgyi
C Cohen

Funding

MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR01AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1986 to 2012
$7.6M
REGULATORY DOMAIN/S1 CRYSTAL STRUCTURE--SCALLOP MYOSINR01AR041808 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1995 to 1999
–
MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR37AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1990 to 1999
–
NIAMS NIH HHS AR17346NIAMS NIH HHS AR41808NIAMS NIH HHS R01 AR017346NIAMS NIH HHS R37 AR017346
6 · The paper itself

Abstract

Here we report a 2.3-A crystal structure of scallop myosin S1 complexed with ADP.BeF(x), as well as three additional structures (at 2.8-3.8 A resolution) for this S1 complexed with ATP analogs, some of which are cross-linked by para-phenyl dimaleimide, a short intramolecular cross-linker. In all cases, the complexes are characterized by an unwound SH1 helix first seen in an unusual 2.5-A scallop myosin-MgADP structure and described as corresponding to a previously unrecognized actin-detached internally uncoupled state. The unwinding of the SH1 helix effectively uncouples the converter/lever arm module from the motor and allows cross-linking by para-phenyl dimaleimide, which has been shown to occur only in weak actin-binding states of the molecule. Mutations near the metastable SH1 helix that disable the motor can be accounted for by viewing this structural element as a clutch controlling the transmission of torque to the lever arm. We have also determined a 3.2-A nucleotide-free structure of scallop myosin S1, which suggests that in the near-rigor state there are two conformations in the switch I loop, depending on whether nucleotide is present. Analysis of the subdomain motions in the weak actin-binding states revealed by x-ray crystallography, together with recent electron microscopic results, clarify the mechanical roles of the parts of the motor in the course of the contractile cycle and suggest how strong binding to actin triggers both the power stroke and product release.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCrystallography, X-RayElectronsModels, MolecularMolluscaMyosinsProtein BindingProtein ConformationProtein Structure, TertiaryAdenosine DiphosphateAdenosine TriphosphateMyosins

Identifiers

PMID12297624
PMCPMC130514

What OpenQuestion holds

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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.