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7KFL

Crystal structure of the cargo-binding domain from the plant class XI myosin (MyoXIk)

7KFL の概要
エントリーDOI10.2210/pdb7kfl/pdb
分子名称Myosin-17 (2 entities in total)
機能のキーワードclass xi myosin, cargo-binding domain, motor protein
由来する生物種Arabidopsis thaliana (Mouse-ear cress)
タンパク質・核酸の鎖数2
化学式量合計89348.41
構造登録者
主引用文献Turowski, V.R.,Ruiz, D.M.,Nascimento, A.F.Z.,Millan, C.,Sammito, M.D.,Juanhuix, J.,Cremonesi, A.S.,Uson, I.,Giuseppe, P.O.,Murakami, M.T.
Structure of the class XI myosin globular tail reveals evolutionary hallmarks for cargo recognition in plants.
Acta Crystallogr D Struct Biol, 77:522-533, 2021
Cited by
PubMed Abstract: The plant-specific class XI myosins (MyoXIs) play key roles at the molecular, cellular and tissue levels, engaging diverse adaptor proteins to transport cargoes along actin filaments. To recognize their cargoes, MyoXIs have a C-terminal globular tail domain (GTD) that is evolutionarily related to those of class V myosins (MyoVs) from animals and fungi. Despite recent advances in understanding the functional roles played by MyoXI in plants, the structure of its GTD, and therefore the molecular determinants for cargo selectivity and recognition, remain elusive. In this study, the first crystal structure of a MyoXI GTD, that of MyoXI-K from Arabidopsis thaliana, was elucidated at 2.35 Å resolution using a low-identity and fragment-based phasing approach in ARCIMBOLDO_SHREDDER. The results reveal that both the composition and the length of the α5-α6 loop are distinctive features of MyoXI-K, providing evidence for a structural stabilizing role for this loop, which is otherwise carried out by a molecular zipper in MyoV GTDs. The crystal structure also shows that most of the characterized cargo-binding sites in MyoVs are not conserved in plant MyoXIs, pointing to plant-specific cargo-recognition mechanisms. Notably, the main elements involved in the self-regulation mechanism of MyoVs are conserved in plant MyoXIs, indicating this to be an ancient ancestral trait.
PubMed: 33825712
DOI: 10.1107/S2059798321001583
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.35 Å)
構造検証レポート
Validation report summary of 7kfl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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