A phosphate-binding pocket within the platform-PAZ-connector helix cassette of human Dicer

Mol Cell. 2014 Feb 20;53(4):606-16. doi: 10.1016/j.molcel.2014.01.003. Epub 2014 Jan 30.

Abstract

We have solved two families of crystal structures of the human Dicer "platform-PAZ-connector helix" cassette in complex with small interfering RNAs (siRNAs). The structures possess two adjacently positioned pockets: a 2 nt 3'-overhang-binding pocket within the PAZ domain (3' pocket) and a phosphate-binding pocket within the platform domain (phosphate pocket). One family of complexes contains a knob-like α-helical protrusion, designated "hDicer-specific helix," that separates the two pockets and orients the bound siRNA away from the surface of Dicer, which could be indicative of a product release/transfer state. In the second complex, the helical protrusion is melted/disordered and the bound siRNA is aligned toward the surface of Dicer, suggestive of a cleavage-competent state. These structures allow us to propose that the transition from the cleavage-competent to the postulated product release/transfer state may involve release of the 5'-phosphate from the phosphate pocket while retaining the 3' overhang in the 3' pocket.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cells, Cultured
  • Crystallography, X-Ray
  • DEAD-box RNA Helicases / chemistry*
  • DEAD-box RNA Helicases / metabolism
  • Humans
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Mutation
  • Phosphates / chemistry
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Small Interfering / metabolism
  • Ribonuclease III / chemistry*
  • Ribonuclease III / metabolism
  • Sequence Homology, Amino Acid
  • Surface Plasmon Resonance

Substances

  • Phosphates
  • RNA, Small Interfering
  • DICER1 protein, human
  • Ribonuclease III
  • DEAD-box RNA Helicases