4KP3

Crystal Structure of MyoVa-GTD in Complex with Two Cargos

4KP3 の概要

• エントリーDOI: 10.2210/pdb4kp3/pdb
• 関連するPDBエントリー: 3WB8
• 分子名称: Unconventional myosin-Va, RILP-like protein 2, Melanophilin, ... (4 entities in total)
• 機能のキーワード: helix bundle, motor protein-protein transport complex, motor protein/protein transport
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm, cytosol : Q99LE1; Melanosome: Q91V27
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 125193.13

構造登録者

Wei, Z.,Liu, X.,Yu, C.,Zhang, M. (登録日: 2013-05-13, 公開日: 2013-07-10, 最終更新日: 2023-11-08)

主引用文献

Wei, Z.,Liu, X.,Yu, C.,Zhang, M.
Structural basis of cargo recognitions for class V myosins
Proc.Natl.Acad.Sci.USA, 110:11314-11319, 2013

PubMed Abstract: Class V myosins (MyoV), the most studied unconventional myosins, recognize numerous cargos mainly via the motor's globular tail domain (GTD). Little is known regarding how MyoV-GTD recognizes such a diverse array of cargos specifically. Here, we solved the crystal structures of MyoVa-GTD in its apo-form and in complex with two distinct cargos, melanophilin and Rab interacting lysosomal protein-like 2. The apo-MyoVa-GTD structure indicates that most mutations found in patients with Griscelli syndrome, microvillus inclusion disease, or cancers or in "dilute" rodents likely impair the folding of GTD. The MyoVa-GTD/cargo complex structure reveals two distinct cargo-binding surfaces, one primarily via charge-charge interaction and the other mainly via hydrophobic interactions. Structural and biochemical analysis reveal the specific cargo-binding specificities of various isoforms of mammalian MyoV as well as very different cargo recognition mechanisms of MyoV between yeast and higher eukaryotes. The MyoVa-GTD structures resolved here provide a framework for future functional studies of vertebrate class V myosins.

PubMed: 23798443
DOI: 10.1073/pnas.1306768110

実験手法

X-RAY DIFFRACTION (2.405 Å)