3MMI

Crystal structure of the globular tail of Myo4p

Summary for 3MMI

• Entry DOI: 10.2210/pdb3mmi/pdb
• Descriptor: Myosin-4 (2 entities in total)
• Functional Keywords: globular tail, type v myosin, dilute domain, motor protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Bud: P32492
• Total number of polymer chains: 2
• Total formula weight: 87973.87

Authors

Heuck, A.,Niessing, D. (deposition date: 2010-04-19, release date: 2010-05-12, Last modification date: 2024-02-21)

Primary citation

Heuck, A.,Fetka, I.,Brewer, D.N.,Huls, D.,Munson, M.,Jansen, R.P.,Niessing, D.
The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.
J.Cell Biol., 189:497-510, 2010

PubMed Abstract: Type V myosin (MyoV)-dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2-tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail-lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.

PubMed: 20439999
DOI: 10.1083/jcb.201002076

Experimental method

X-RAY DIFFRACTION (2.3 Å)