Intrinsic dynamics is evolutionarily optimized to enable allosteric behavior
نویسندگان
چکیده
منابع مشابه
Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation.
In recent years, there has been a surge in the number of studies exploring the relationship between proteins' equilibrium dynamics and structural changes involved in function. An emerging concept, supported by both theory and experiments, is that under native state conditions proteins have an intrinsic ability to sample conformations that meet functional requirements. A typical example is the a...
متن کاملStructures of pyruvate kinases display evolutionarily divergent allosteric strategies
The transition between the inactive T-state (apoenzyme) and active R-state (effector bound enzyme) of Trypanosoma cruzi pyruvate kinase (PYK) is accompanied by a symmetrical 8° rigid body rocking motion of the A- and C-domain cores in each of the four subunits, coupled with the formation of additional salt bridges across two of the four subunit interfaces. These salt bridges provide increased t...
متن کاملMechanosensation is evolutionarily tuned to locomotor mechanics.
The biomechanics of animal limbs has evolved to meet the functional demands for movement associated with different behaviors and environments. Effective movement relies not only on limb mechanics but also on appropriate mechanosensory feedback. By comparing sensory ability and mechanics within a phylogenetic framework, we show that peripheral mechanosensation has evolved with limb biomechanics,...
متن کاملIs altruism evolutionarily stable
We develop an evolutionary approach to explain altruistic preferences. Given their preferences, individuals interact rationally with each other. By comparing the success of players with different preferences, we investigate whether evolution favors altruistic or selfish attitudes. The outcome depends on whether the individuals' interactions are strategic complements or substitutes. Altruism and...
متن کاملEscherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer.
In this contribution the kinetic mechanism and substrate specificity of Escherichia coli diacylglycerol kinase were examined. Steady state kinetic studies were carried out under mixed micellar conditions using a novel continuous coupled assay system. The kinetic data were consistent with a random equilibrium mechanism, implying that diacylglycerol kinase catalyzes direct phosphoryl transfer fro...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Current Opinion in Structural Biology
سال: 2020
ISSN: 0959-440X
DOI: 10.1016/j.sbi.2019.11.002