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  • Gardino, Alexandra K (author)

Transient Non-native Hydrogen Bonds Promote Activation of a Signaling Protein

  • Article/chapterEnglish2009

Publisher, publication year, extent ...

  • Elsevier BV,2009
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-30235
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-30235URI
  • https://doi.org/10.1016/j.cell.2009.11.022DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • SummaryPhosphorylation is a common mechanism for activating proteins within signaling pathways. Yet, the molecular transitions between the inactive and active conformational states are poorly understood. Here we quantitatively characterize the free-energy landscape of activation of a signaling protein, nitrogen regulatory protein C (NtrC), by connecting functional protein dynamics of phosphorylation-dependent activation to protein folding and show that only a rarely populated, pre-existing active conformation is energetically stabilized by phosphorylation. Using nuclear magnetic resonance (NMR) dynamics, we test an atomic scale pathway for the complex conformational transition, inferred from molecular dynamics simulations (Lei et al., 2009). The data show that the loss of native stabilizing contacts during activation is compensated by non-native transient atomic interactions during the transition. The results unravel atomistic details of native-state protein energy landscapes by expanding the knowledge about ground states to transition landscapes.

Added entries (persons, corporate bodies, meetings, titles ...)

  • Villali, Janice (author)
  • Kivenson, Aleksandr (author)
  • Lei, Ming (author)
  • Liu, Ce Feng (author)
  • Steindel, Phillip (author)
  • Eisenmesser, Elan Z (author)
  • Labeikovsky, Wladimir (author)
  • Wolf-Watz, MagnusUmeå universitet,Kemiska institutionen(Swepub:umu)maswoz04 (author)
  • Clarkson, Michael W (author)
  • Kern, Dorothee (author)
  • Umeå universitetKemiska institutionen (creator_code:org_t)

Related titles

  • In:Cell: Elsevier BV139:6, s. 1109-180092-86741097-4172

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