A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.

Abstract:

:Myosins are molecular motors that power diverse cellular processes, such as rapid organelle transport, muscle contraction, and tension-sensitive anchoring. The structural adaptations in the motor that allow for this functional diversity are not known, due, in part, to the lack of high-resolution structures of highly tension-sensitive myosins. We determined a 2.3-Å resolution structure of apo-myosin-Ib (Myo1b), which is the most tension-sensitive myosin characterized. We identified a striking unique orientation of structural elements that position the motor's lever arm. This orientation results in a cavity between the motor and lever arm that holds a 10-residue stretch of N-terminal amino acids, a region that is divergent among myosins. Single-molecule and biochemical analyses show that the N terminus plays an important role in stabilizing the post power-stroke conformation of Myo1b and in tuning the rate of the force-sensitive transition. We propose that this region plays a general role in tuning the mechanochemical properties of myosins.

authors

Shuman H,Greenberg MJ,Zwolak A,Lin T,Sindelar CV,Dominguez R,Ostap EM

doi

10.1073/pnas.1321022111

subject

Has Abstract

pub_date

2014-02-11 00:00:00

pages

2116-21

issue

6

eissn

0027-8424

issn

1091-6490

pii

1321022111

journal_volume

111

pub_type

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