Three-dimensional structure of myosin subfragment-1: a molecular motor

TLDR

Directed movement in living organisms results from converting chemical energy into mechanical energy, with myosin being one of three motor families that drive cellular motility. The structure was determined by single‑crystal X‑ray diffraction. The 3D structure of myosin subfragment‑1, including actin and nucleotide binding sites, provides a framework for understanding the molecular basis of motility.

Abstract

Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.