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

doi:10.1126/science.8316857

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

Robert Wood Johnson Medical School (RWJMS), Pathology

Research output: Contribution to journal › Article › peer-review

1877 Scopus citations

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 acting 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 language	English (US)
Pages (from-to)	50-58
Number of pages	9
Journal	Science
Volume	261
Issue number	5117
DOIs	https://doi.org/10.1126/science.8316857
State	Published - 1993

All Science Journal Classification (ASJC) codes

General

Access to Document

10.1126/science.8316857

Cite this

@article{24b2f373873e4b88b65c61440037ac85,

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 acting 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",

doi = "10.1126/science.8316857",

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

Y1 - 1993

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 acting 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 acting 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

U2 - 10.1126/science.8316857

DO - 10.1126/science.8316857

M3 - Article

C2 - 8316857

AN - SCOPUS:0027194702

SN - 0036-8075

VL - 261

SP - 50

EP - 58

JO - Science

JF - Science

IS - 5117

ER -

Three-dimensional structure of myosin subfragment-1: A molecular motor

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this