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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)1310-1315
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number11
DOIs
StatePublished - Nov 2011

Keywords

  • membrane dynamics
  • mitochondria
  • peroxisomes
  • protein-protein interactions
  • tail-anchoring
  • tetratricopeptide repeats

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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