Asset Details

  • Description:
  • Model of α10 helix‐mediated activation of DevR. Unphosphorylated WT DevR forms a dimer through the α5/α6 dimeric interface (‘Interface I’). Phosphorylation (Phos) of D54 residue in the receiver domain (REC) triggers conformational rearrangements, resulting in a switch of the dimeric interface from ‘Interface I’ to ‘Interface II’ (α10/α10), leading to the formation of active dimer species, cooperative binding of DevR to DNA (D, C and P sites) and transcription by RNA polymerase (RNAP). hspX is shown as a representative target gene of the DevR regulon. Unphosphorylated DevR∆α10 also forms an inactive dimer through ‘Interface I’. However, as a result of dissolution of ‘Interface I’ post‐phosphorylation (Hyper phos. REC) and the absence of α10 helix, ‘Interface II’ (active dimer) is not generated in DevR∆α10, resulting in DNA‐binding and gene activation defects. Only relevant regions of the protein are shown to clarify the mechanism.
  • License:
  • Rights Managed
  • Rights Holder:
  • John Wiley & Sons, Inc.
  • License Rights Holder:
  • Copyright © 2016 Federation of European Biochemical Societies
  • Asset Type:
  • Image
  • Asset Subtype:
  • Figure
  • Image Orientation:
  • Landscape
  • Image Dimensions:
  • 2128 x 1499
  • Image File Size:
  • 472 KB
  • Creator:
  • Atul Vashist, D. Prithvi Raj, Umesh Datta Gupta, Rajiv Bhat, Jaya Sivaswami Tyagi
  • Credit:
  • Vashist, A., Prithvi Raj, D., Gupta, U. D., Bhat, R., & Tyagi, J. S. (2016). The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity. The FEBS Journal, 283(7), 1286-1299..
  • Collection:
  • Keywords:
  • Restrictions:
  • Property Release:
  • No
  • Model Release:
  • No
  • Purchasable:
  • Yes
  • Sensitive Materials:
  • No
  • Article Authors:
  • Atul Vashist, D. Prithvi Raj, Umesh Datta Gupta, Rajiv Bhat, Jaya Sivaswami Tyagi
  • Article Copyright Year:
  • 2016
  • Publication Volume:
  • 283
  • Publication Issue:
  • 7
  • Publication Date:
  • 04/01/2016
  • DOI:

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