2KIA

Solution structure of Myosin VI C-terminal cargo-binding domain

2KIA の概要

• エントリーDOI: 10.2210/pdb2kia/pdb
• 分子名称: Myosin-VI (1 entity in total)
• 機能のキーワード: myosin vi, cargo-binding domain, molecular motor, actin-binding, atp-binding, calmodulin-binding, cell projection, coated pit, coiled coil, cytoplasm, cytoplasmic vesicle, deafness, disease mutation, endocytosis, golgi apparatus, hearing, membrane, motor protein, myosin, nucleotide-binding, nucleus, phosphoprotein, protein transport, transport
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q64331
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15385.69

構造登録者

Feng, W.,Yu, C.,Wei, Z.,Miyanoiri, Y.,Zhang, M. (登録日: 2009-04-29, 公開日: 2009-09-29, 最終更新日: 2024-05-29)

主引用文献

Yu, C.,Feng, W.,Wei, Z.,Miyanoiri, Y.,Wen, W.,Zhao, Y.,Zhang, M.
Myosin VI undergoes cargo-mediated dimerization
Cell(Cambridge,Mass.), 138:537-548, 2009

PubMed Abstract: Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.

PubMed: 19665975
DOI: 10.1016/j.cell.2009.05.030

実験手法

SOLUTION NMR