Evidence map›Paper›PMID 11226153›Full record

ArticleThe EMBO journal2001

Structure of a genetically engineered molecular motor.

W Kliche, S Fujita-Becker, M Kollmar, D J Manstein, F J Kull

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017
    Article
  6. Review
  7. ATP turnover by individual myosin molecules hints at two conformers of the myosin active site.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Functional characterization of the human myosin-7a motor domain.Cellular and molecular life sciences : CMLS · 2012
    Article
  12. Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  13. Article
  14. Article
  15. Thioredoxin as a fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2008
    Article
  16. Article
  17. Article
  18. The stroke size of myosins: a reevaluation.Journal of muscle research and cell motility · 2006
    Review
  19. Molecular engineering of myosin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    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

5 authors at 1 institution in 1 country.

W KlicheDepartment of Biophysics, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. kull@mpimf-heidelberg.mpg.de
S Fujita-Becker
M Kollmar
D J Manstein
F J Kull
Max Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the nucleotide-binding region into force-generating movements of larger protein domains. We present the 2.8 A resolution crystal structure of an artificial actin-based motor. By combining the catalytic domain of myosin II with a 130 A conformational amplifier consisting of repeats 1 and 2 of alpha-actinin, we demonstrate that it is possible to genetically engineer single-polypeptide molecular motors with precisely defined lever arm lengths and specific motile properties. Furthermore, our structure shows the consequences of mutating a conserved salt bridge in the nucleotide-binding region. Disruption of this salt bridge, which is known to severely inhibit ATP hydrolysis activity, appears to interfere with formation of myosin's catalytically active 'closed' conformation. Finally, we describe the structure of alpha-actinin repeats 1 and 2 as being composed of two rigid, triple-helical bundles linked by an uninterrupted alpha-helix. This fold is very similar to the previously described structures of alpha-actinin repeats 2 and 3, and alpha-spectrin repeats 16 and 17.

Indexed as

ActininCrystallography, X-RayModels, MolecularMolecular Motor ProteinsProtein ConformationProtein EngineeringProtein Structure, SecondaryRecombinant ProteinsActininMolecular Motor ProteinsRecombinant Proteins

Identifiers

PMID11226153
PMCPMC140180
OpenAlexW2158093004

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.