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Unlike myosin, kinesin proteins only function in a homodimer form, suggesting that coupling between the two protomers is essential for the functional cycle of kinesin.
A symmetric interface is formed via the same kind of interactions between the two protomers.
When engaged with LapG, this perfect symmetry between the two protomers observed in the apo-state is broken.
(A ) One lipid molecule (PE, green) in the cavity between the two protomers in the dimer contributes to the hydrophobic contacts across the dimer interface.
However, the effect of these interactions needs to be interpreted with caution since the conformations of the A´α helices differ between the two protomers.
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Structural variation between the sequences within the two protomers in the crystallographic X-ray structure was gauged by calculating segmental RMSD (per residue) of protomer A relative to protomer B. Resulting RMSD values for PDC109/a, PDC109/b and the linker are 0.009, 0.019, and 0.030, respectively.
Val21 not only mediates coiled-coil interactions between A′α helices of the two protomers but also interacts with Phe105 in Hβ of the partner protomer.
It is worthy to note that the transition between these two stages is different for the two protomers, with one much earlier than the other.
One characteristic feature of the AcrB trimer is the absolute requirement of functional cooperation between the three protomers (Eicher et al. 2014).
Because of cooperativity between the three protomers, the intrinsic conformational energy terms, ∆G C1/2/3, and energy terms for cooperativity work, W C1/2/3, shown in B cancel each other out.
The loop regions following this until residue 185 differ in structure between the four protomers of the crystal asymmetric unit.
More suggestions(15)
between the two countries
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between the two versions
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between the two camps
between the two shuffles
between the two arches
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