6IXQ

Structure of Myo2-GTD in complex with Smy1

Summary for 6IXQ

• Entry DOI: 10.2210/pdb6ixq/pdb
• Descriptor: Myosin-2, Kinesin-related protein SMY1 (2 entities in total)
• Functional Keywords: cargo binding domain, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 53769.77

Authors

Tang, K.,Wei, Z. (deposition date: 2018-12-11, release date: 2019-03-06, Last modification date: 2023-11-22)

Primary citation

Tang, K.,Li, Y.,Yu, C.,Wei, Z.
Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.
J.Biol.Chem., 294:5896-5906, 2019

PubMed Abstract: Class V myosins are actin-dependent motors, which recognize numerous cellular cargos mainly via the C-terminal globular tail domain (GTD). Myo2, a yeast class V myosin, can transport a broad range of organelles. However, little is known about the capacity of Myo2-GTD to recognize such a diverse array of cargos specifically at the molecular level. Here, we solved crystal structures of Myo2-GTD (at 1.9-3.1 Å resolutions) in complex with three cargo adaptor proteins: Smy1 (for polarization of secretory vesicles), Inp2 (for peroxisome transport), and Mmr1 (for mitochondria transport). The structures of Smy1- and Inp2-bound Myo2-GTD, along with site-directed mutagenesis experiments, revealed a binding site in subdomain-I having a hydrophobic groove with high flexibility enabling Myo2-GTD to accommodate different protein sequences. The Myo2-GTD-Mmr1 complex structure confirmed and complemented a previously identified mitochondrion/vacuole-specific binding region. Moreover, differences between the conformations and locations of cargo-binding sites identified here for Myo2 and those reported for mammalian MyoVA (MyoVA) suggest that class V myosins potentially have co-evolved with their specific cargos. Our structural and biochemical analysis not only uncovers a molecular mechanism that explains the diverse cargo recognition by Myo2-GTD, but also provides structural information useful for future functional studies of class V myosins in cargo transport.

PubMed: 30804213
DOI: 10.1074/jbc.RA119.007550

Experimental method

X-RAY DIFFRACTION (3.06 Å)