Ontology highlight
ABSTRACT:
SUBMITTER: Focia PJ
PROVIDER: S-EPMC3546161 | biostudies-literature | 2004 Jan
REPOSITORIES: biostudies-literature
Focia Pamela J PJ Shepotinovskaya Irina V IV Seidler James A JA Freymann Douglas M DM
Science (New York, N.Y.) 20040101 5656
Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symmetric heterodimer sequestering a composite active site that contains two bound nucleotides. The structure explains the coordinate activation of the two GTPases. Conformational changes coupled to forma ...[more]