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PDBsum entry 4pjm
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Motor protein
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PDB id
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4pjm
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DOI no:
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Dev Cell
33:401-412
(2015)
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PubMed id:
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How actin initiates the motor activity of Myosin.
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P.Llinas,
T.Isabet,
L.Song,
V.Ropars,
B.Zong,
H.Benisty,
S.Sirigu,
C.Morris,
C.Kikuti,
D.Safer,
H.L.Sweeney,
A.Houdusse.
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ABSTRACT
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Fundamental to cellular processes are directional movements driven by molecular
motors. A common theme for these and other molecular machines driven by ATP is
that controlled release of hydrolysis products is essential for using the
chemical energy efficiently. Mechanochemical transduction by myosin motors on
actin is coupled to unknown structural changes that result in the sequential
release of inorganic phosphate (Pi) and MgADP. We present here a myosin
structure possessing an actin-binding interface and a tunnel (back door) that
creates an escape route for Pi with a minimal rotation of the myosin lever arm
that drives movements. We propose that this state represents the beginning of
the powerstroke on actin and that Pi translocation from the nucleotide pocket
triggered by actin binding initiates myosin force generation. This elucidates
how actin initiates force generation and movement and may represent a strategy
common to many molecular machines.
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');
}
}
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