Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh.

ABSTRACT: The NG domain of the prokaryotic signal recognition protein Ffh is a two-domain GTPase that comprises part of the prokaryotic signal recognition particle (SRP) that functions in co-translational targeting of proteins to the membrane. The interface between the N and G domains includes two highly conserved sequence motifs and is adjacent in sequence and structure to one of the conserved GTPase signature motifs. Previous structural studies have shown that the relative orientation of the two domains is dynamic. The N domain of Ffh has been proposed to function in regulating the nucleotide-binding interactions of the G domain. However, biochemical studies suggest a more complex role for the domain in integrating communication between signal sequence recognition and interaction with receptor. He

SUBMITTER: Ramirez UD 

PROVIDER: S-EPMC3542393 | biostudies-literature | 2002 Jul

REPOSITORIES: biostudies-literature