2XU6

MDV1 coiled coil domain

2XU6 の概要

• エントリーDOI: 10.2210/pdb2xu6/pdb
• 分子名称: MDV1 COILED COIL (2 entities in total)
• 機能のキーワード: protein binding, mitochondrial outer membrane, adapter protein, organelle division
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side: P47025
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17072.62

構造登録者

Koirala, S.,Bui, H.T.,Schubert, H.L.,Eckert, D.M.,Hill, C.P.,Kay, M.S.,Shaw, J.M. (登録日: 2010-10-14, 公開日: 2010-10-27, 最終更新日: 2024-11-06)

主引用文献

Koirala, S.,Bui, H.T.,Schubert, H.L.,Eckert, D.M.,Hill, C.P.,Kay, M.S.,Shaw, J.M.
Molecular Architecture of a Dynamin Adaptor: Implications for Assembly of Mitochondrial Fission Complexes
J.Cell Biol., 191:1127-, 2010

PubMed Abstract: Recruitment 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-Å 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 β-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.

PubMed: 21149566
DOI: 10.1083/JCB.201005046

実験手法

X-RAY DIFFRACTION (2.7 Å)