The backrub motion: how protein backbone shrugs when a sidechain dances.

Published

Journal Article

Surprisingly, the frozen structures from ultra-high-resolution protein crystallography reveal a prevalent, but subtle, mode of local backbone motion coupled to much larger, two-state changes of sidechain conformation. This "backrub" motion provides an influential and common type of local plasticity in protein backbone. Concerted reorientation of two adjacent peptides swings the central sidechain perpendicular to the chain direction, changing accessible sidechain conformations while leaving flanking structure undisturbed. Alternate conformations in sub-1 angstroms crystal structures show backrub motions for two-thirds of the significant Cbeta shifts and 3% of the total residues in these proteins (126/3882), accompanied by two-state changes in sidechain rotamer. The Backrub modeling tool is effective in crystallographic rebuilding. For homology modeling or protein redesign, backrubs can provide realistic, small perturbations to rigid backbones. For large sidechain changes in protein dynamics or for single mutations, backrubs allow backbone accommodation while maintaining H bonds and ideal geometry.

Full Text

Duke Authors

Cited Authors

  • Davis, IW; Arendall, WB; Richardson, DC; Richardson, JS

Published Date

  • February 2006

Published In

Volume / Issue

  • 14 / 2

Start / End Page

  • 265 - 274

PubMed ID

  • 16472746

Pubmed Central ID

  • 16472746

Electronic International Standard Serial Number (EISSN)

  • 1878-4186

International Standard Serial Number (ISSN)

  • 0969-2126

Digital Object Identifier (DOI)

  • 10.1016/j.str.2005.10.007

Language

  • eng