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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 11(67), p. 1310-1315, 2011

DOI: 10.1107/s1744309111029368

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The 1.75 Å resolution structure of fission protein Fis1 fromSaccharomyces cerevisiaereveals elusive interactions of the autoinhibitory domain

Journal article published in 2011 by James E. Tooley, Victor Khangulov, Jonathan P. B. Lees, Jamie L. Schlessman, Maria C. Bewley, Annie Heroux, Jürgen Bosch ORCID, R. Blake Hill
This paper is available in a repository.
This paper is available in a repository.

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Abstract

Fis1 mediates mitochondrial and peroxisomal fission. It is tail-anchored to these organelles by a transmembrane domain, exposing a soluble cytoplasmic domain. Previous studies suggested that Fis1 is autoinhibited by its N-terminal region. Here, a 1.75 Å resolution crystal structure of the Fis1 cytoplasmic domain from Saccharomyces cerevisiae is reported which adopts a tetratricopeptide-repeat fold. It is observed that this fold creates a concave surface important for fission, but is sterically occluded by its N-terminal region. Thus, this structure provides a physical basis for autoinhibition and allows a detailed examination of the interactions that stabilize the inhibited state of this molecule.