Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation

Ivet Bahar, Chakra Chennubhotla, Dror Tobi

Research output: Contribution to journalReview articlepeer-review

260 Scopus citations

Abstract

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 ability of enzymes to sample open and closed forms, irrespective of substrate, succeeded by the stabilization of one form (usually closed) upon substrate binding. This ability is structure-encoded, and plays a key role in facilitating allosteric regulation, which suggests complementing the sequence-encodes-structure paradigm of protein science by structure-encodes-dynamics-encodes-function. The emerging connection implies an evolutionary role in selecting/conserving structures based on their ability to achieve functional dynamics, and in turn, selecting sequences that fold into such 'apt' structures.

Original languageEnglish
Pages (from-to)633-640
Number of pages8
JournalCurrent Opinion in Structural Biology
Volume17
Issue number6
DOIs
StatePublished - Dec 2007
Externally publishedYes

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