4J5L

Structure of the Cargo Binding Domain from Human Myosin Va

Summary for 4J5L

• Entry DOI: 10.2210/pdb4j5l/pdb
• Related: 4J5M
• Descriptor: Unconventional myosin-Va, SULFATE ION (3 entities in total)
• Functional Keywords: human myosin va, c-terminal globular tail, intracellular traffic, vesicles, protein transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 93670.48

Authors

Nascimento, A.F.Z.,Trindade, D.M.,Tonoli, C.C.C.,Assis, L.H.P.,Mahajan, P.,Berridge, G.,Krojer, T.,Vollmar, M.,Burgess-Brown, N.,von Delft, F.,Murakami, M.T. (deposition date: 2013-02-08, release date: 2013-10-09, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)