2PQR
Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4
Summary for 2PQR
Entry DOI | 10.2210/pdb2pqr/pdb |
Related | 2PQN |
Descriptor | Mitochondria fission 1 protein, WD repeat protein YKR036C, GOLD ION, ... (4 entities in total) |
Functional Keywords | tpr domain, protein-protein complex, apoptosis |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Mitochondrion outer membrane ; Single-pass membrane protein : P40515 Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side : P36130 |
Total number of polymer chains | 4 |
Total formula weight | 44946.44 |
Authors | Zhang, Y.,Chan, D.C. (deposition date: 2007-05-02, release date: 2007-11-06, Last modification date: 2023-08-30) |
Primary citation | Zhang, Y.,Chan, D.C. Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc.Natl.Acad.Sci.USA, 104:18526-18530, 2007 Cited by PubMed Abstract: Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using crystallographic analysis of adaptor-Fis1 complexes, we show that these adaptors use two helices to bind to both the concave and convex surfaces of the Fis1 TPR domain. Fis1 therefore contains two interaction interfaces, a binding mode that, to our knowledge, has not been observed previously for TPR domains. Genetic and biochemical studies indicate that both binding interfaces are important for binding of Mdv1 and Caf4 to Fis1 and for mitochondrial fission activity in vivo. Our results reveal how Fis1 recruits the mitochondrial fission complex and will facilitate efforts to manipulate mitochondrial fission. PubMed: 17998537DOI: 10.1073/pnas.0706441104 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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