2pqn | pdb_00002pqn

Crystal structure of yeast Fis1 complexed with a fragment of yeast Mdv1

spinqualitylabelsall models 2pqn, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pqn is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2pqr Gene: FIS1, MDV2 (ATCC 18824), MDV1, FIS2, GAG3, NET2 (ATCC 18824) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FIS1_YEAST] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division. [MDV1_YEAST] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for recruitment of mitochondrial fission complexes by Fis1.,Zhang Y, Chan DC Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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