4xco

Publication Abstract from PubMed

Co-translational protein targeting is an essential, evolutionarily conserved pathway for delivering nascent proteins to the proper cellular membrane. In this pathway, the signal recognition particle (SRP) first recognizes the N-terminal signal sequence of nascent proteins and subsequently interacts with the SRP receptor. For this, signal sequence binding in the SRP54 M domain must be effectively communicated to the SRP54 NG domain that interacts with the receptor. Here we present the 2.9 A crystal structure of unbound- and signal sequence bound SRP forms, both present in the asymmetric unit. The structures provide evidence for a coupled binding and folding mechanism in which signal sequence binding induces the concerted folding of the GM linker helix, the finger loop, and the C-terminal alpha helix alphaM6. This mechanism allows for a high degree of structural adaptability of the binding site and suggests how signal sequence binding in the M domain is coupled to repositioning of the NG domain.

Signal-sequence induced conformational changes in the signal recognition particle.,Hainzl T, Sauer-Eriksson AE Nat Commun. 2015 Jun 8;6:7163. doi: 10.1038/ncomms8163. PMID:26051119^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.