1lkx

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1lkx, resolution 3.00Å

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MOTOR DOMAIN OF MYOE, A CLASS-I MYOSIN

Overview

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.

About this Structure

1LKX is a Single protein structure of sequence from Dictyostelium discoideum with MG, VO4 and ADP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the motor domain of a class-I myosin., Kollmar M, Durrwang U, Kliche W, Manstein DJ, Kull FJ, EMBO J. 2002 Jun 3;21(11):2517-25. PMID:12032065

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