1okk
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HOMO-HETERODIMERIC COMPLEX OF THE SRP GTPASES
OverviewOverview
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 formation, of their extensive interface may function allosterically to signal, formation of the targeting complex to the signal-sequence binding site and, the translocon. We propose that the complex represents a molecular "latch", and that its disengagement is regulated by completion of assembly of the, GTPase active site.
About this StructureAbout this Structure
1OKK is a Protein complex structure of sequences from Thermus aquaticus with SO4, MG, GCP, BZP and EDO as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Heterodimeric GTPase core of the SRP targeting complex., Focia PJ, Shepotinovskaya IV, Seidler JA, Freymann DM, Science. 2004 Jan 16;303(5656):373-7. PMID:14726591
Page seeded by OCA on Tue Dec 18 17:48:32 2007