3UUX

Crystal structure of yeast Fis1 in complex with Mdv1 fragment containing N-terminal extension and coiled coil domains

Summary for 3UUX

• Entry DOI: 10.2210/pdb3uux/pdb
• Related: 2PQN 2PQR 2XU6
• Descriptor: Mitochondria fission 1 protein, Mitochondrial division protein 1 (2 entities in total)
• Functional Keywords: tetratricopeptide repeat, mitochondrial fission, mitochondria and cytoplasm, apoptosis
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast); More
• Cellular location: Mitochondrion outer membrane; Single-pass membrane protein: P40515; Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side: P47025
• Total number of polymer chains: 4
• Total formula weight: 84542.56

Authors

Zhang, Y.,Chan, N.C.,Gristick, H.,Chan, D.C. (deposition date: 2011-11-28, release date: 2012-02-08, Last modification date: 2024-10-16)

Primary citation

Zhang, Y.,Chan, N.C.,Ngo, H.B.,Gristick, H.,Chan, D.C.
Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (mdv1) coiled coil.
J.Biol.Chem., 287:9855-9861, 2012

PubMed Abstract: The mitochondrial fission machinery is best understood in the yeast Saccharomyces cerevisiae, where Fis1, Mdv1, and Dnm1 are essential components. Fis1 is a mitochondrial outer membrane protein that recruits the dynamin-related GTPase Dnm1 during the fission process. This recruitment occurs via Mdv1, which binds both Fis1 and Dnm1 and therefore functions as a molecular adaptor linking the two molecules. Mdv1 has a modular structure, consisting of an N-terminal extension that binds Fis1, a central coiled coil for dimerization, and a C-terminal WD40 repeat region that binds Dnm1. We have solved the crystal structure of a dimeric Mdv1-Fis1 complex that contains both the N-terminal extension and coiled-coil regions of Mdv1. Consistent with previous studies, Mdv1 binds Fis1 through a U-shaped helix-loop-helix motif, and dimerization of the Mdv1-Fis1 complex is mediated by the antiparallel coiled coil of Mdv1. However, the complex is surprisingly compact and rigid due to two additional contacts mediated by the surface of the Mdv1 coiled coil. The coiled coil packs against both Fis1 and the second helix of the Mdv1 helix-loop-helix motif. Mutational analyses showed that these contacts are important for mitochondrial fission activity. These results indicate that, in addition to dimerization, the unusually long Mdv1 coiled coil serves a scaffolding function to stabilize the Mdv1-Fis1 complex.

PubMed: 22303011
DOI: 10.1074/jbc.M111.329359

Experimental method

X-RAY DIFFRACTION (3.9 Å)