Biomolecular Motors
Biomolecular Motors
Biomolecular Motors
• Motion is accomplished by diffusion and capture, without the need for directed motion
• Motors are employed for micrometer and meter scale movement- separation
of chromosomes, remodeling of cell organelles, contraction of our muscles etc.
Myosin
Myosin
• Motor domain is elongated with a site for binding ATP- Catalytic domain
• At rest its bend and can accept an ATP and holds the actin
• ATP is hydrolysed when the Pi vacates it straigtens- Power stroke and
dissociates fro actin
• The different cargo in catalytic site changes the relay loops which acts on the
converter domain- bringing about a larger change
• Change is amplified by lever arm a major shift of 100A 0
Motor domain
• Different cargo (ATP/ADP) on the motor make a linker a Neck linker ordered or disordered
• Two sensor loops that constitute the relay helix – transduces information
• ATP cleaved, Pi hydrogen bond in the catalytic site- A switch- when the interaction is
is broken
Kinesin
ATP synthase
• F1 is composed of a ring of six subunits, three alpha subunits and three beta subunits
• An axle runs through the center of the ring, pressing differently on the three
beta subunits and changing their structure.
• The different conformations of the -subunit have markedly different affinity for ATP.
• Each rotation of 120° occurs in two steps
• When rotation is powered by ATP, a 90° rotation happens
• The ATP then hydrolyzes into ADP.. the dissociation of ADP then fuels a 30° rotation.
• The movement is reversible
• The forcible rotation of the axle first increases the affinity for ADP,
which combines with phosphate to form ATP without change in conformation,
and further rotation forces ATP to be released.
• In proton pump- The F1 rotes by ATP hydrolysis
• When acting as a motor, ATP is easy to bind to the motor but difficult to release
and ADP is difficult to bind but easy to release.
Flagellar motor