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

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-angstrom 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 degrees flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.