| Literature DB >> 17498971 |
Ewald M Aydt1, Gerhard Wolff, Ingo Morano.
Abstract
Type II myosin is the molecular motor which drives contraction upon cyclic interaction with filamentous actin while consuming ATP. The contemporary crystallographic structure of the myosin subfragment-1 (S1) of myosin covers both the motor domain of the heavy chain (MHC) as well as the essential (ELC) and regulatory light chains (RLC). A part of the N-terminus of the ELC is, however, missing in the 3D-models of Type II myosin. The N-terminal domain of the ELC comprises interesting functional features since it binds to actin thus controlling myosin motor activity. For the first time, we modeled the missing 46 N-terminal amino acid of the ELC to the contemporary actin-myosin-S1 complex. We show a rod-like 91 A structure being long enough to bridge the gap between the ELC core of myosin-S1 and the appropriate binding site of the ELC on the actin filament.Entities:
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Year: 2007 PMID： 17498971 DOI： 10.1016/j.jsb.2007.04.002
Source DB: PubMed Journal: J Struct Biol ISSN： 1047-8477 Impact factor: 2.867