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2PQR

Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4

Summary for 2PQR
Entry DOI10.2210/pdb2pqr/pdb
Related2PQN
DescriptorMitochondria fission 1 protein, WD repeat protein YKR036C, GOLD ION, ... (4 entities in total)
Functional Keywordstpr domain, protein-protein complex, apoptosis
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationMitochondrion outer membrane ; Single-pass membrane protein : P40515
Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side : P36130
Total number of polymer chains4
Total formula weight44946.44
Authors
Zhang, Y.,Chan, D.C. (deposition date: 2007-05-02, release date: 2007-11-06, Last modification date: 2023-08-30)
Primary citationZhang, 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: 17998537
DOI: 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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数据于2024-12-25公开中

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