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x * 22400-25600, recombinant M-domain of subunit SRP54, SDS-PAGE and SAXS
dimer
subunit SRP54, X-ray crystallography
heterodimer
-
cpSRP54-cpFtsY complex
heterodimer
-
1 * 54000 + 1 * 43000, chloroplast signal recognition particle is a heterodimer consisting of a 54 kDa GTPase (cpSRP54) subunit, and a 43 kDa subunit (cpSRP43)
heterodimer
1 * 54000 + 1 * 43000, chloroplast signal recognition particle protein is a heterodimer formed by the subunits cpSRP54 and cpSRP43, X-ray crystallography
heterodimer
-
cpSRP lacks an RNA moiety and functions as a heterodimer composed of a conserved 54-kDa guanosine triphosphatase (cpSRP54) and a unique 43-kDa subunit (cpSRP43)
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
heterodimer
P61010; P06625
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
heterodimer
-
Ffh and FtsY associate into a heterodimer upon GTP binding, upon GTP hydrolysis Ffh and FtsY dissociate
heterodimer
-
Ffh-FtsY complex
heterodimer
-
SRP-FtsY complex
heterodimer
-
SRP-SR complex
heterodimer
P08240; Q9Y5M8
-
heterodimer
P08240; Q9Y5M8
1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE
heterodimer
Q9DBG7; P47758
1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE
heterodimer
Thermochaetoides thermophila
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
heterodimer
Thermochaetoides thermophila CBS 144.50
-
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
-
heterodimer
Thermochaetoides thermophila DSM 1495
-
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
-
heterodimer
Thermochaetoides thermophila IMI 039719
-
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
-
heterodimer
-
Ffh-FtsY complex
heterodimer
-
FtsY and Ffh assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex
heterodimer
-
SRP-SR complex
homodimer
-
-
homodimer
subunit SRP14, X-ray crystallography
monomer
-
gel filtration
monomer
-
gel filtration
-
monomer
Thermochaetoides thermophila
SRbeta is a small monomeric GTPase
monomer
Thermochaetoides thermophila CBS 144.50
-
SRbeta is a small monomeric GTPase
-
monomer
Thermochaetoides thermophila DSM 1495
-
SRbeta is a small monomeric GTPase
-
monomer
Thermochaetoides thermophila IMI 039719
-
SRbeta is a small monomeric GTPase
-
additional information
-
homology modeling and structure analysis, overview
additional information
P61010; P06625
determination of the crystal structure of the GTPase heterodimers, and structure comparisons, overview
additional information
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. Biochemical analysis and integrative modeling suggest that the homodimer employs the same interface as the heterodimer. Ffh does not homodimerize while FtsY is able to form a homodimer. FtsY homodimer and FtsY/Ffh heterodimer share a similar interface
additional information
-
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. Biochemical analysis and integrative modeling suggest that the homodimer employs the same interface as the heterodimer. Ffh does not homodimerize while FtsY is able to form a homodimer. FtsY homodimer and FtsY/Ffh heterodimer share a similar interface
additional information
P08240; Q9Y5M8
in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases
additional information
Q9DBG7; P47758
in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases