title: Crystal structure of the motor domain of a class-I myosin.
abstract: The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently resolved molecules, highlighting regions that undergo large conformational changes. Differences are particularly pronounced in the actin binding region and the converter domain. The changes in position of the converter domain reflect movements both parallel to and perpendicular to the actin axis. The orientation of the converter domain is approximately 30 degrees further up than in other myosin structures, indicating that MyoE can produce a larger power stroke by rotating its lever arm through a larger angle. The role of extended loops near the actin-binding site is discussed in the context of cellular localization. The core regions of the motor domain are similar, and the structure reveals how that core is stabilized in the absence of an N-terminal SH3-like domain.
authors.affiliation: Department of Biophysics, Max Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Kollmar
authors.forename: Ulrike
authors.initials: U
authors.lastname: Dürrwang
authors.forename: Werner
authors.initials: W
authors.lastname: Kliche
authors.forename: Dietmar J
authors.initials: DJ
authors.lastname: Manstein
authors.forename: F Jon
authors.initials: FJ
authors.lastname: Kull
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004023:Dictyostelium / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D018482:Muscle, Skeletal / Q000378:metabolism; D024461:Myosin Type I / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D018909:src Homology Domains
chemical_list: D000199:Actins; D024461:Myosin Type I