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1okk
From Proteopedia
Revision as of 13:53, 28 September 2014 by OCA (Talk | contribs)
1okk is a 2 chain structure with sequence from Thermus aquaticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
