2q9c
Structure of FTSY:GMPPNP with MGCL Complex
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OverviewOverview
The signal recognition particle (SRP) and its conjugate receptor (SR), mediate cotranslational targeting of a subclass of proteins destined for, secretion to the endoplasmic reticulum membrane in eukaryotes or to the, plasma membrane in prokaryotes. Conserved active site residues in the, GTPase domains of both SRP and SR mediate discrete conformational changes, during formation and dissociation of the SRP.SR complex. Here, we describe, structures of the prokaryotic SR, FtsY, as an apo protein and in two, different complexes with a non-hydrolysable GTP analog (GMPPNP). These, structures reveal intermediate conformations of FtsY containing GMPPNP and, explain how the conserved active site residues position the nucleotide, into a non-catalytic conformation. The basis for the lower specificity of, binding of nucleotide in FtsY prior to heterodimerization with the SRP, conjugate Ffh is also shown. We propose that these structural changes, represent discrete conformational states assumed by FtsY during targeting, complex formation and dissociation.
About this StructureAbout this Structure
2Q9C is a Single protein structure of sequence from Thermus aquaticus with SO4 and GNP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
X-ray Structures of the Signal Recognition Particle Receptor Reveal Targeting Cycle Intermediates., Reyes CL, Rutenber E, Walter P, Stroud RM, PLoS ONE. 2007 Jul 11;2:e607. PMID:17622352
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