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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.

SUBMITTER: Kollmar M

PROVIDER: S-EPMC126035 | biostudies-literature | 2002 Jun

REPOSITORIES: biostudies-literature

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Crystal structure of the motor domain of a class-I myosin.

Kollmar Martin M Dürrwang Ulrike U Kliche Werner W Manstein Dietmar J DJ Kull F Jon FJ

The EMBO journal 20020601 11

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 o ...[more]

PMID: 12032065

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