Three-dimensional structure of myosin subfragment-1

A molecular motor

Ivan Rayment, Wojciech R. Rypniewski, Karen Schmidt-Bäse, Robert Smith, Diana R. Tomchick, Matthew M. Benning, Donald A. Winkelmann, Gary Wesenberg, Hazel M. Holden

Research output: Contribution to journalArticle

1764 Citations (Scopus)

Abstract

Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

Original languageEnglish (US)
Pages (from-to)50-58
Number of pages9
JournalScience
Volume261
Issue number5117
StatePublished - Jul 2 1993

Fingerprint

Myosin Subfragments
Myosins
Molecular Structure
Actins
Nucleotides
Binding Sites
Head
X-Rays

ASJC Scopus subject areas

  • General

Cite this

Rayment, I., Rypniewski, W. R., Schmidt-Bäse, K., Smith, R., Tomchick, D. R., Benning, M. M., ... Holden, H. M. (1993). Three-dimensional structure of myosin subfragment-1: A molecular motor. Science, 261(5117), 50-58.

Three-dimensional structure of myosin subfragment-1 : A molecular motor. / Rayment, Ivan; Rypniewski, Wojciech R.; Schmidt-Bäse, Karen; Smith, Robert; Tomchick, Diana R.; Benning, Matthew M.; Winkelmann, Donald A.; Wesenberg, Gary; Holden, Hazel M.

In: Science, Vol. 261, No. 5117, 02.07.1993, p. 50-58.

Research output: Contribution to journalArticle

Rayment, I, Rypniewski, WR, Schmidt-Bäse, K, Smith, R, Tomchick, DR, Benning, MM, Winkelmann, DA, Wesenberg, G & Holden, HM 1993, 'Three-dimensional structure of myosin subfragment-1: A molecular motor', Science, vol. 261, no. 5117, pp. 50-58.
Rayment I, Rypniewski WR, Schmidt-Bäse K, Smith R, Tomchick DR, Benning MM et al. Three-dimensional structure of myosin subfragment-1: A molecular motor. Science. 1993 Jul 2;261(5117):50-58.
Rayment, Ivan ; Rypniewski, Wojciech R. ; Schmidt-Bäse, Karen ; Smith, Robert ; Tomchick, Diana R. ; Benning, Matthew M. ; Winkelmann, Donald A. ; Wesenberg, Gary ; Holden, Hazel M. / Three-dimensional structure of myosin subfragment-1 : A molecular motor. In: Science. 1993 ; Vol. 261, No. 5117. pp. 50-58.
@article{a3b479f4c8e74b9c8671d42e3cc1043a,
title = "Three-dimensional structure of myosin subfragment-1: A molecular motor",
abstract = "Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.",
author = "Ivan Rayment and Rypniewski, {Wojciech R.} and Karen Schmidt-B{\"a}se and Robert Smith and Tomchick, {Diana R.} and Benning, {Matthew M.} and Winkelmann, {Donald A.} and Gary Wesenberg and Holden, {Hazel M.}",
year = "1993",
month = "7",
day = "2",
language = "English (US)",
volume = "261",
pages = "50--58",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5117",

}

TY - JOUR

T1 - Three-dimensional structure of myosin subfragment-1

T2 - A molecular motor

AU - Rayment, Ivan

AU - Rypniewski, Wojciech R.

AU - Schmidt-Bäse, Karen

AU - Smith, Robert

AU - Tomchick, Diana R.

AU - Benning, Matthew M.

AU - Winkelmann, Donald A.

AU - Wesenberg, Gary

AU - Holden, Hazel M.

PY - 1993/7/2

Y1 - 1993/7/2

N2 - Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

AB - Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

UR - http://www.scopus.com/inward/record.url?scp=0027194702&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027194702&partnerID=8YFLogxK

M3 - Article

VL - 261

SP - 50

EP - 58

JO - Science

JF - Science

SN - 0036-8075

IS - 5117

ER -