2xu6 | pdb_00002xu6
MDV1 COILED COIL DOMAIN
Structural highlights
Function[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.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedRecruitment and assembly of some dynamin-related guanosine triphosphatases depends on adaptor proteins restricted to distinct cellular membranes. The yeast Mdv1 adaptor localizes to mitochondria by binding to the membrane protein Fis1. Subsequent Mdv1 binding to the mitochondrial dynamin Dnm1 stimulates Dnm1 assembly into spirals, which encircle and divide the mitochondrial compartment. In this study, we report that dimeric Mdv1 is joined at its center by a 92-A antiparallel coiled coil (CC). Modeling of the Fis1-Mdv1 complex using available crystal structures suggests that the Mdv1 CC lies parallel to the bilayer with N termini at opposite ends bound to Fis1 and C-terminal beta-propeller domains (Dnm1-binding sites) extending into the cytoplasm. A CC length of appropriate length and sequence is necessary for optimal Mdv1 interaction with Fis1 and Dnm1 and is important for proper Dnm1 assembly before membrane scission. Our results provide a framework for understanding how adaptors act as scaffolds to orient and stabilize the assembly of dynamins on membranes. Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes.,Koirala S, Bui HT, Schubert HL, Eckert DM, Hill CP, Kay MS, Shaw JM J Cell Biol. 2010 Dec 13;191(6):1127-39. PMID:21149566[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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