3O48

Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae

Summary for 3O48

• Entry DOI: 10.2210/pdb3o48/pdb
• Related: 1iyg 1nzn 1pc2 1y8m 2pqn 2pqr
• Descriptor: Mitochondria fission 1 protein (2 entities in total)
• Functional Keywords: tetratricopeptide repeat fold, tpr, scaffold, mitochondria, peroxisome, membrane fission, protein binding
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Cellular location: Mitochondrion outer membrane; Single-pass membrane protein: P40515
• Total number of polymer chains: 1
• Total formula weight: 15840.05

Authors

Tooley, J.E.,Khangulov, V.,Heroux, A.,Bosch, J.,Hill, R.B. (deposition date: 2010-07-26, release date: 2011-08-10, Last modification date: 2023-09-06)

Primary citation

Tooley, J.E.,Khangulov, V.,Lees, J.P.,Schlessman, J.L.,Bewley, M.C.,Heroux, A.,Bosch, J.,Hill, R.B.
The 1.75 Angstrom resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain
Acta Crystallogr.,Sect.F, 67:1310-1315, 2011

PubMed 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.

PubMed: 22102223
DOI: 10.1107/S1744309111029368

Experimental method

X-RAY DIFFRACTION (1.75 Å)