Structural highlights
Function
[MYOE_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. May play a role in moving membranes relative to actin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kollmar M, Durrwang U, Kliche W, Manstein DJ, Kull FJ. Crystal structure of the motor domain of a class-I myosin. EMBO J. 2002 Jun 3;21(11):2517-25. PMID:12032065 doi:10.1093/emboj/21.11.2517
