Protein conformational disorder and enzyme catalysis

Top Curr Chem. 2013:337:41-67. doi: 10.1007/128_2012_411.

Abstract

Though lacking a well-defined three-dimensional structure, intrinsically unstructured proteins are ubiquitous in nature. These molecules play crucial roles in many cellular processes, especially signaling and regulation. Surprisingly, even enzyme catalysis can tolerate substantial disorder. This observation contravenes conventional wisdom but is relevant to an understanding of how protein dynamics modulates enzyme function. This chapter reviews properties and characteristics of disordered proteins, emphasizing examples of enzymes that lack defined structures, and considers implications of structural disorder for catalytic efficiency and evolution.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Catalysis
  • Enzymes / chemistry
  • Enzymes / metabolism
  • Evolution, Chemical
  • Intrinsically Disordered Proteins / chemistry*
  • Intrinsically Disordered Proteins / metabolism
  • Protein Binding
  • Protein Conformation

Substances

  • Enzymes
  • Intrinsically Disordered Proteins