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An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-α-mannanase inhibitor.

Tyson BelzYi JinJoan CoinesCarme RoviraGideon J DaviesSpencer J Williams
Published in: Chemical communications (Cambridge, England) (2017)
The non-hydrolyzable S-linked azasugars, 1,6-α-mannosylthio- and 1,6-α-mannobiosylthioisofagomine, were synthesized and shown to bind with high affinity to a family 76 endo-1,6-α-mannanase from Bacillus circulans. X-ray crystallography showed an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener.
Keyphrases
  • molecular dynamics simulations
  • molecular docking
  • high resolution
  • genome wide
  • single cell
  • computed tomography
  • gene expression
  • magnetic resonance
  • mass spectrometry
  • crystal structure
  • dual energy
  • bacillus subtilis