4LLI

Crystal Structure of human Myosin 5a globular domain

Summary for 4LLI

• Entry DOI: 10.2210/pdb4lli/pdb
• Related: 4LNZ
• Descriptor: Unconventional myosin-Va (2 entities in total)
• Functional Keywords: globular tail, type v myosin, dilute domain, motor protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 90326.82

Authors

Velvarska, H.,Niessing, D. (deposition date: 2013-07-09, release date: 2013-12-25, Last modification date: 2024-02-28)

Primary citation

Velvarska, H.,Niessing, D.
Structural insights into the globular tails of the human type v myosins myo5a, myo5b, and myo5c.
Plos One, 8:e82065-e82065, 2013

PubMed Abstract: Vertebrate type V myosins (MyoV) Myo5a, Myo5b, and Myo5c mediate transport of several different cargoes. All MyoV paralogs bind to cargo complexes mainly by their C-terminal globular domains. In absence of cargo, the globular domain of Myo5a inhibits its motor domain. Here, we report low-resolution SAXS models for the globular domains from human Myo5a, Myo5b, and Myo5c, which suggest very similar overall shapes of all three paralogs. We determined the crystal structures of globular domains from Myo5a and Myo5b, and provide a homology model for human Myo5c. When we docked the Myo5a crystal structure into a previously published electron microscopy density of the autoinhibited full-length Myo5a, only one domain orientation resulted in a good fit. This structural arrangement suggests the participation of additional region of the globular domain in autoinhibition. Quantification of the interaction of the Myo5a globular domain with its motor complex revealed a tight binding with dissociation half-life in the order of minutes, suggesting a rather slow transition between the active and inactive states.

PubMed: 24339992
DOI: 10.1371/journal.pone.0082065

Experimental method

X-RAY DIFFRACTION (2.2 Å)