A new structural state of myosin.

Published

Journal Article (Review)

The mechanism by which motor proteins hydrolyze ATP and move along cytoskeletal filaments is still unknown. One approach to deciphering the mechanism is to correlate steps of ATP hydrolysis with structural states of the motors to determine the changes the motors undergo during the hydrolysis cycle. Unfortunately, available crystal structures represent only a few steps of the cycle and obtaining atomic structures that represent the motors bound to their filament has been difficult. Now, two new myosin crystal structures have been reported that show features expected for myosin motors bound in rigor to actin. The two new structures show changes at both the actin-binding surface and the active site that have not been observed previously.

Full Text

Duke Authors

Cited Authors

  • Kull, FJ; Endow, SA

Published Date

  • March 2004

Published In

Volume / Issue

  • 29 / 3

Start / End Page

  • 103 - 106

PubMed ID

  • 15055201

Pubmed Central ID

  • 15055201

International Standard Serial Number (ISSN)

  • 0968-0004

Digital Object Identifier (DOI)

  • 10.1016/j.tibs.2004.01.001

Language

  • eng