The Structure of Crystalline Profilin–β-actin

Authors

Nalin Goonesekere, Princeton UniversityFollow
Clarence E. Schutt, Princeton University
James C. Myslik, Princeton University
Michael D. Rozycki, Princeton University
Uno Lindberg, Stockholm UniversityFollow

Document Type

Article

Journal/Book/Conference Title

nature

Volume

365

First Page

810

Last Page

816

Abstract

The three-dimensional structure of bovine profilin–β-actin has been solved to 2.55 Å resolution by X-ray crystallography. There are several significant local changes in the structure of β-actin compared with α-actin as well as an overall 5° rotation between its two major domains. Actin molecules in the crystal are organized into ribbons through intermolecular contacts like those found in oligomeric protein assemblies. Profilin forms two extensive contacts with the actin ribbon, one of which appears to correspond to the solution contact in vitro.

Department

Department of Chemistry and Biochemistry

Original Publication Date

10-28-1993

DOI of published version

10.1038/365810a0

Recommended Citation

Goonesekere, Nalin; Schutt, Clarence E.; Myslik, James C.; Rozycki, Michael D.; and Lindberg, Uno, "The Structure of Crystalline Profilin–β-actin" (1993). Faculty Publications. 6324.
https://scholarworks.uni.edu/facpub/6324