EC Number   |
Subunits |
Reference |
|---|
   3.6.5.4 | heterodimer |
FtsY and Ffh assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex |
689926 |
| 3.6.5.4 | heterodimer |
SRP GTPases are multi-domain proteins. SRalpha consists of an N-terminal SNARE-like Longin domain (SRX domain) that is connected by a long flexible linker to the NG domain, which harbors the GTPase activity. The SRX domain is responsible for interaction with the SRbeta GTPase in a GTP-dependent manner |
-, 758481 |
| 3.6.5.4 | heterodimer |
SRP-FtsY complex |
687902, 687905 |
| 3.6.5.4 | heterodimer |
SRP-SR complex |
686249 |
| 3.6.5.4 | heterodimer |
the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane. Determination of in silico three-dimensional model of the structure of cpSRP54 by homology modeling using cytosolic homologues. Single-molecule Foerster resonance energy transfer experiments reveals the presence of at least two distinct conformations. Small angle X-ray scattering shows that the linking region among the GTPase (G-domain) and methionine-rich (M-domain) domains, an M-domain loop, and the cpSRP43 binding C-terminal extension of cpSRP54 are predominantly disordered. The linker and loop segments are observed to play an important role in organizing the domain arrangement of cpSRP54. Domain structure, overview. The orientation of the M-domain varies in different SRP54s and bacterial homologues Ffhs, structure comparisons of wild-type and mutants and enzyme from other species, detailed overview. Subunit cpSRP54 exists in at least two different conformations |
756198 |
| 3.6.5.4 | heterodimer |
the signal recognition particle (SRP) receptor is a heterodimer of two polypeptides (SRalpha and SRbeta) that each contain a GTP binding domain. The GTP binding domain in the peripheral membrane SRalpha subunit has a well defined role in regulating targeting of SRP ribosome-nascent chain complexes to the translocon. Without bound GTP, the empty form of the SRbeta GTPase domain is unable to dimerize with SRalpha |
757430 |
| 3.6.5.4 | homodimer |
- |
686396 |
| 3.6.5.4 | homodimer |
subunit SRP14, X-ray crystallography |
695328 |
| 3.6.5.4 | monomer |
gel filtration |
-, 644172 |
| 3.6.5.4 | monomer |
SRbeta is a small monomeric GTPase |
-, 758481 |
