Structural basis of signal-sequence recognition by the signal recognition particle

Nat Struct Mol Biol. 2011 Mar;18(3):389-91. doi: 10.1038/nsmb.1994. Epub 2011 Feb 20.

Abstract

The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180° flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism*
  • Base Sequence
  • Crystallography, X-Ray
  • Methanococcus / chemistry
  • Methanococcus / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Sorting Signals*
  • Signal Recognition Particle / chemistry*
  • Signal Recognition Particle / metabolism*

Substances

  • Archaeal Proteins
  • Protein Sorting Signals
  • Signal Recognition Particle