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Picometer-scale conformational heterogeneity separates functional from nonfunctional states of a photoreceptor protein

Academic Article
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Overview

authors

  • Coureux, P. D.
  • Fan, Z. P.
  • Stojanoff, V.
  • Genick, Ulrich

publication date

  • June 2008

journal

  • Structure  Journal

abstract

  • Protein structural fluctuations occur over a wide spatial scale, ranging from minute, picometer-scale displacements, to large, interdomain motions and partial unfolding. While large-scale protein structural changes and their effects on protein function have been the focus of much recent attention, small-scale fluctuations have been less well studied, and are generally assumed to have proportionally smaller effects. Here we use the bacterial photoreceptor photoactive yellow protein (PYP) to test if subtle structural changes do, indeed, imply equally subtle functional effects. We flash froze crystals of PYP to trap the protein's conformational ensemble, and probed the molecules in this ensemble for their ability to facilitate PYP's biological function (i.e., light-driven isomerization of its chromophore). Our results indicate that the apparently homogeneous structural state observed in a 0.82 A crystal structure in fact comprises an ensemble of conformational states, in which subpopulations with nearly identical structures display dramatically different functional properties.

subject areas

  • Bacterial Proteins
  • Binding Sites
  • Crystallography, X-Ray
  • Freezing
  • Isomerism
  • Light
  • Models, Molecular
  • Photochemistry
  • Photoreceptors, Microbial
  • Protein Conformation
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Identity

International Standard Serial Number (ISSN)

  • 0969-2126

Digital Object Identifier (DOI)

  • 10.1016/j.str.2008.02.022

PubMed ID

  • 18547519
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Additional Document Info

start page

  • 863

end page

  • 872

volume

  • 16

issue

  • 6

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