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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 11; pp. 1310 - 1315
• Main Authors: Tooley, James E., Khangulov, Victor, Lees, Jonathan P. B., Schlessman, Jamie L., Bewley, Maria C., Heroux, Annie, Bosch, Jürgen, Hill, R. Blake
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.2011
• Subjects: Crystallography, X-Ray; membrane dynamics; mitochondria; Mitochondrial Proteins - chemistry; Models, Molecular; peroxisomes; Protein Interaction Domains and Motifs; protein-protein interactions; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae Proteins - chemistry; Structural Communications; Structural Homology, Protein; tail-anchoring; tetratricopeptide repeats
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309111029368

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.