4J5M

Structure of the Cargo Binding Domain from Human Myosin Vb

4J5M の概要

• エントリーDOI: 10.2210/pdb4j5m/pdb
• 関連するPDBエントリー: 4J5L
• 分子名称: Unconventional myosin-Vb, NITRATE ION (3 entities in total)
• 機能のキーワード: intracellular traffic, organelles, vesicles, human myosin vb, protein transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45634.42

構造登録者

Nascimento, A.F.Z.,Trindade, D.M.,Mahajan, P.,Berridge, G.,Krojer, T.,Vollmar, M.,Tonoli, C.C.C.,Assis, L.H.P.,Burgess-Brown, N.,von Delft, F.,Murakami, M.T. (登録日: 2013-02-08, 公開日: 2013-10-09, 最終更新日: 2024-02-28)

主引用文献

Nascimento, A.F.,Trindade, D.M.,Tonoli, C.C.,de Giuseppe, P.O.,Assis, L.H.,Honorato, R.V.,de Oliveira, P.S.,Mahajan, P.,Burgess-Brown, N.A.,von Delft, F.,Larson, R.E.,Murakami, M.T.
Structural Insights into Functional Overlapping and Differentiation among Myosin V Motors.
J.Biol.Chem., 288:34131-34145, 2013

PubMed Abstract: Myosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes, and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb, and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned, indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high resolution insights into motor domain inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, autoinhibition, and regulatory mechanisms in myosin V motors.

PubMed: 24097982
DOI: 10.1074/jbc.M113.507202

実験手法

X-RAY DIFFRACTION (2.07 Å)