Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1 - PubMed (original) (raw)

. 1993 Jul 8;364(6433):171-4.

doi: 10.1038/364171a0.

Affiliations

• PMID: 8321290
• DOI: 10.1038/364171a0

Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1

R R Schröder et al. Nature. 1993.

Abstract

Elucidation of the molecular contacts between actin and myosin is central to understanding the force-generating process in muscle and other cells. Actin, a highly conserved globular protein found in all eukaryotes, polymerizes into filaments (F-actin) for most of its biological functions. Myosins, which are more diverse in sequence, share a conserved globular head of about 900 amino acids in length (subfragment-1 or S1) at the N-terminal end of the molecule. S1 contains all the elements necessary for mechano-chemical force transduction in vitro. Here we report an atomic model for the actomyosin complex produced by combining the atomic X-ray structure of F-actin and chicken myosin S1 with a three-dimensional reconstruction from electron micrographs of frozen-hydrated F-actin decorated with recombinant Dictyostelium myosin S1. The accuracy of the reconstruction shows the position of actin and myosin molecules unambiguously.

PubMed Disclaimer

Similar articles

• Molecular structure of F-actin and location of surface binding sites.
  Milligan RA, Whittaker M, Safer D. Milligan RA, et al. Nature. 1990 Nov 15;348(6298):217-21. doi: 10.1038/348217a0. Nature. 1990. PMID: 2234090
• Cooperative rigor binding of myosin to actin is a function of F-actin structure.
  Orlova A, Egelman EH. Orlova A, et al. J Mol Biol. 1997 Feb 7;265(5):469-74. doi: 10.1006/jmbi.1996.0761. J Mol Biol. 1997. PMID: 9048941
• A single myosin head can be cross-linked to the N termini of two adjacent actin monomers.
  Bonafé N, Chaussepied P. Bonafé N, et al. Biophys J. 1995 Apr;68(4 Suppl):35S-43S. Biophys J. 1995. PMID: 7787098 Free PMC article.
• Cryo-electron microscopy of S1-decorated actin filaments.
  Flicker PF, Milligan RA, Applegate D. Flicker PF, et al. Adv Biophys. 1991;27:185-96. doi: 10.1016/0065-227x(91)90017-8. Adv Biophys. 1991. PMID: 1755359 Review.
• A comparison of the atomic model of F-actin with cryo-electron micrographs of actin and decorated actin.
  Holmes KC, Tirion M, Popp D, Lorenz M, Kabsch W, Milligan RA. Holmes KC, et al. Adv Exp Med Biol. 1993;332:15-22; discussion 22-4. doi: 10.1007/978-1-4615-2872-2_2. Adv Exp Med Biol. 1993. PMID: 8109328 Review.

Cited by

• Kenneth Charles Holmes 1934-2021.
  Bullard B. Bullard B. Front Mol Biosci. 2022 Mar 18;9:855014. doi: 10.3389/fmolb.2022.855014. eCollection 2022. Front Mol Biosci. 2022. PMID: 35372521 Free PMC article. No abstract available.
• Structural basis of Fusarium myosin I inhibition by phenamacril.
  Zhou Y, Zhou XE, Gong Y, Zhu Y, Cao X, Brunzelle JS, Xu HE, Zhou M, Melcher K, Zhang F. Zhou Y, et al. PLoS Pathog. 2020 Mar 12;16(3):e1008323. doi: 10.1371/journal.ppat.1008323. eCollection 2020 Mar. PLoS Pathog. 2020. PMID: 32163521 Free PMC article.
• Porcine myosin-VI: characterization of a new mammalian unconventional myosin.
  Hasson T, Mooseker MS. Hasson T, et al. J Cell Biol. 1994 Oct;127(2):425-40. doi: 10.1083/jcb.127.2.425. J Cell Biol. 1994. PMID: 7929586 Free PMC article.
• Myosin-induced changes in F-actin: fluorescence probing of subdomain 2 by dansyl ethylenediamine attached to Gln-41.
  Kim E, Miller CJ, Motoki M, Seguro K, Muhlrad A, Reisler E. Kim E, et al. Biophys J. 1996 Mar;70(3):1439-46. doi: 10.1016/S0006-3495(96)79703-5. Biophys J. 1996. PMID: 8785300 Free PMC article.
• From amoeboid myosin to unique targeted medicines for a genetic cardiac disease.
  Spudich JA. Spudich JA. Front Physiol. 2024 Oct 28;15:1496569. doi: 10.3389/fphys.2024.1496569. eCollection 2024. Front Physiol. 2024. PMID: 39529926 Free PMC article. Review.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Nature Publishing Group