The 1.75 Å resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain.

James E Tooley, Victor Khangulov, Jonathan P B Lees, Jamie L Schlessman, Maria C Bewley, Annie Heroux, Jürgen Bosch, R Blake Hill

Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.

Acta crystallographica. Section F, Structural biology and crystallization communications 2011 Nov 1

filter terms:

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. © 2011 International Union of Crystallography. All rights reserved.

Citation

James E Tooley, Victor Khangulov, Jonathan P B Lees, Jamie L Schlessman, Maria C Bewley, Annie Heroux, Jürgen Bosch, R Blake Hill. The 1.75 Å resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain. Acta crystallographica. Section F, Structural biology and crystallization communications. 2011 Nov 1;67(Pt 11):1310-5