Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Relay/converter conformation

The relay/converter conformation is the readout of the result of these inputs. In going from the post-rigor to pre-power states, the only signal is SW2 going from open to closed, which produces the relay kink and the converter up. To go from the pre-power to rigor states requires the /i-twist, which is triggered by actin binding and cleft closure. [Pg.178]

Fig. 3. Details of the seven-stranded /1-sheet and associated structures (A and B) in the post-rigor conformation and (C and D) in the pre-powerstroke conformation. The orientation of A and C is at right angles to that shown in Fig. 2. When attached to actin, it corresponds to that shown in Fig. 5B. The colors are as in Fig. 2. The views shown in B and D are at right angles to A and C looking out radially from the axis of the actin helix. Note the kink in the relay helix shown in C and D that leads to a 60° rotation of the converter domain. This in turn rotates the lever arm 60°. The P-loop (which constitutes the ATP-binding site) and the adjoining a-helix are shown in yellow. The flanking switch sequences (1 and 2) are also shown. The strands of the /1-sheet are numbered from the N-terminal (distal) end of the sheet. The lower part of strand 5 (light blue) constitutes switch 2. In the post-rigor state, switch 2 lies out of the plane of the /1-sheet (open) and in the pre-powerstroke state switch 2 is in the plane of the /1-sheet (closed). Fig. 3. Details of the seven-stranded /1-sheet and associated structures (A and B) in the post-rigor conformation and (C and D) in the pre-powerstroke conformation. The orientation of A and C is at right angles to that shown in Fig. 2. When attached to actin, it corresponds to that shown in Fig. 5B. The colors are as in Fig. 2. The views shown in B and D are at right angles to A and C looking out radially from the axis of the actin helix. Note the kink in the relay helix shown in C and D that leads to a 60° rotation of the converter domain. This in turn rotates the lever arm 60°. The P-loop (which constitutes the ATP-binding site) and the adjoining a-helix are shown in yellow. The flanking switch sequences (1 and 2) are also shown. The strands of the /1-sheet are numbered from the N-terminal (distal) end of the sheet. The lower part of strand 5 (light blue) constitutes switch 2. In the post-rigor state, switch 2 lies out of the plane of the /1-sheet (open) and in the pre-powerstroke state switch 2 is in the plane of the /1-sheet (closed).

See other pages where Relay/converter conformation is mentioned: [Pg.31]    [Pg.250]    [Pg.167]    [Pg.177]    [Pg.179]    [Pg.182]    [Pg.330]    [Pg.333]    [Pg.1400]    [Pg.176]    [Pg.647]    [Pg.25]    [Pg.26]    [Pg.26]    [Pg.30]    [Pg.40]    [Pg.42]    [Pg.399]    [Pg.175]    [Pg.148]   
See also in sourсe #XX -- [ Pg.178 ]




SEARCH



© 2024 chempedia.info