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PDBsum entry 5ejq
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Motor protein
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PDB id
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5ejq
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References listed in PDB file
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Key reference
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Title
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Myosin myth4-Ferm structures highlight important principles of convergent evolution.
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Authors
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V.J.Planelles-Herrero,
F.Blanc,
S.Sirigu,
H.Sirkia,
J.Clause,
Y.Sourigues,
D.O.Johnsrud,
B.Amigues,
M.Cecchini,
S.P.Gilbert,
A.Houdusse,
M.A.Titus.
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Ref.
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Proc Natl Acad Sci U S A, 2016,
113,
E2906.
[DOI no: ]
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PubMed id
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Abstract
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Myosins containing MyTH4-FERM (myosin tail homology 4-band 4.1, ezrin, radixin,
moesin, or MF) domains in their tails are found in a wide range of
phylogenetically divergent organisms, such as humans and the social amoeba
Dictyostelium (Dd). Interestingly, evolutionarily distant MF myosins have
similar roles in the extension of actin-filled membrane protrusions such as
filopodia and bind to microtubules (MT), suggesting that the core functions of
these MF myosins have been highly conserved over evolution. The structures of
two DdMyo7 signature MF domains have been determined and comparison with
mammalian MF structures reveals that characteristic features of MF domains are
conserved. However, across millions of years of evolution conserved
class-specific insertions are seen to alter the surfaces and the orientation of
subdomains with respect to each other, likely resulting in new sites for binding
partners. The MyTH4 domains of Myo10 and DdMyo7 bind to MT with micromolar
affinity but, surprisingly, their MT binding sites are on opposite surfaces of
the MyTH4 domain. The structural analysis in combination with comparison of
diverse MF myosin sequences provides evidence that myosin tail domain features
can be maintained without strict conservation of motifs. The results illustrate
how tuning of existing features can give rise to new structures while preserving
the general properties necessary for myosin tails. Thus, tinkering with the MF
domain enables it to serve as a multifunctional platform for cooperative
recruitment of various partners, allowing common properties such as
autoinhibition of the motor and microtubule binding to arise through convergent
evolution.
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