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3.6.5.4: signal-recognition-particle GTPase

This is an abbreviated version!
For detailed information about signal-recognition-particle GTPase, go to the full flat file.

Word Map on EC 3.6.5.4

Reaction

GTP
+
H2O
=
GDP
 +
phosphate

Synonyms

54-kDa GTPase, chloroplast signal recognition particle, chloroplast signal recognition particle protein, chloroplast signal recognition particle receptor, chloroplast SRP, cpFtsY, cpSRP, cpSRP43, cpSRP54, CtSR, EC 3.6.1.49, Ffh, FlhF, FtsH, FtsY, FtsY GTPase, GTPase, guanine triphosphatase, guanosine 5'-triphosphatase, guanosine triphosphatase, PAB0955, ribosomal GTPase, signal recognition particle, signal recognition particle 54 kDa protein, signal recognition particle receptor, signal recognition particle receptor beta subunit, signal recognition particle receptor subunit alpha, signal recognition particle receptor subunit beta, signal recognition particle-like GTPase, signal-recognition-particle GTPase, SR, SR GTPase, SRalpha, SRbeta, SRbeta GTPase, SRP, SRP GTPase, SRP GTPase Ffh, SRP receptor, SRP receptor GTPase, SRP14, SRP19, SRP21, SRP54, SRP54 GTPase, Srp72p, SRP:SR GTPase, SRP:SR guanine triphosphatase, SRPRA, SRPRB

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.5 Acting on GTP to facilitate cellular and subcellular movement
                3.6.5.4 signal-recognition-particle GTPase

Crystallization

Crystallization on EC 3.6.5.4 - signal-recognition-particle GTPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit cpSRP43 in complex with a synthetic L18 peptide, hanging drop vapour diffusion method, using
the crystal structure of cpFtsY at 2.0 A resolution is reported
-
the crystal structure of cpFtsY with bound malonate is solved at 1.75 A resolution
-
SRalpha and SRbeta complex, X-ray diffraction structure determination and analysis
P61010; P06625
purified recombinant isolated FtsYNG domain in the nucleotide-free (apo) form, the GDP-bound, and the non-hydrolysable GTP-bound form (including GMPPNP (5'-guanylyl imidodiphosphate) and GMPPCP (beta,gamma-methyleneguanosine 5'-triphosphate)), X-ray diffraction structure determination and analysis at 1.22-1.88 A resolution
signal recognition particle in complex with its receptor, X-ray diffraction structure determination and analysis at 3.94 A resolution
-
hanging drop vapor diffusion method, 2.45 A crystal structure of the mammalian SRbeta in its Mg2+GTP-bound state in complex with the minimal binding domain of SRalpha termed SRX
-
crystal structure of the S-domain of signal-recognition-particle RNA at 2.6 A
-
hanging drop vapor diffusion method, 2.45 A crystal structure of the mammalian SRbeta in its Mg2+GTP-bound state in complex with the minimal binding domain of SRalpha termed SRX
-
ammonium sulfate precipitation or sodium citrate precipitation, structures of the NG domain of FtsY in two different forms: an apo and a sulfate-loaded form
-
the crystal structure of PAB0955, free and in complex with six different nucleotides, is determined
-
free and GDP-magnesium-bound forms, hanging drop vapour diffusion method, the hexagonal form grows in 1.1-1.5 M ammonium phosphate and 100 mM sodium acetate pH 5.0. The monoclinic form grows in 0.9-1.2 M lithium sulfate, 0.4-0.6 M ammonium sulfate, and 100 mM sodium citrate pH 5.0. For the GDP-bound structure, best crystals grow in 14-17% (w/v) PEG 8000 and 100 mM Tris pH 8.0
GDP-bound subunit SRP54 and free subunit SRP19 are crystallized by hanging drop vapour diffusion method, crystals of SRP54 grow in 1.0-1.3 M lithium sulfate and 100 mM sodium acetate pH 5.0, crystals of SRP19 grow in 1.2-1.3 M sodium malonate and 100 mM sodium acetate pH 5.0
crystal structure of SRP54 with and without its cognate RNA binding site
-
hanging drop vapour diffusion method, at 21°C, using 50 mM cacodylic acid pH 6.5, 22% (w/v) PEG 4000, and 50 mM sodium acetate
purified recombinant SRbeta in complex with the SRX domain of SRalpha in the GTP-bound state and of GDP- and GDP-Mg2+-bound SRbeta, X-ray diffraction structure determination and analysis at 1.9-3.2 A resolution
Thermochaetoides thermophila
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
-
the 2.1 A X-ray structure of FtsY from Thermus aquaticus bound to GDP is reported
-
the structure of the GMPPNP-stabilized complex of Thermus aquaticus Ffh and FtsY NG domains is determined at 1.97 A resolution
-
two structures of the SRP GTPase Ffh NG-domains are determined at 1.1 A resolution providing the basis for comparative examination of the extensive water structure of the apo conformation
-
X-ray structure of a complex of the N and G domains of Ffh with the GTPase FtsY of the SRP receptor in the presence of the non-hydrolyzable GTP analogue GMPPCP
-