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EC Number
Natural Substrates
Commentary (Nat. Sub.)
GDP + H2O
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GTP + H2O
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GTP + H2O
cotranslational protein targeting to the plasma membrane, the Ffh-4.5S RNA ribonucleoprotein complex and the FtsY protein, respectively, form a unique complex in which both Ffh and FtsY act as GTPase activating proteins for one another, resulting in a mutual stimulation of GTP hydrolysis by both proteins, 4.5S RNA modulates the conformation of the Ffh-FtsY complex and may regulate its GTPase activity during the SRP functional cycle
GTP + H2O
Ffh mediates SRP-dependent, cotranslational protein targeting to the plasma membrane, Ffh and FtsY, the latter being the GTPase subunit of the bacterial SRP receptor, act as GTPase activating proteins for one another, resulting in reciprocal stimulation of GTP hydrolysis
GTP + H2O
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each other’s GTPase activity, they interact only in a primed conformation which requires interdomain communication
GTP + H2O
protein targeting to the plasma membrane
GTP + H2O
protein targeting to the plasma membrane, signal recognition particle cycle, SRP and its receptor stimulate each other’s GTPase activity, GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane
GTP + H2O
the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle
GTP + H2O
the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate
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FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
Results 1 - 10 of 15 > >>