Signal recognition particle receptor: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 2: Line 2:


'''Signal recognition particle receptor''' (SRPR) is associated with the endoplasmic reticulum.  SRPR is a receptor for the [[Signal recognition particle protein|signal recognition particle (SRP)]].  SRPR is a heterodimer with α and β subunits which contain a GTP-binding domain.  SRPR α subunit binds to SRP54 subunit of SRP complex.  SRPR β subunit is a transmembrane GTPase.  The bacterial SRPR is called '''FtsY'''.
'''Signal recognition particle receptor''' (SRPR) is associated with the endoplasmic reticulum.  SRPR is a receptor for the [[Signal recognition particle protein|signal recognition particle (SRP)]].  SRPR is a heterodimer with α and β subunits which contain a GTP-binding domain.  SRPR α subunit binds to SRP54 subunit of SRP complex.  SRPR β subunit is a transmembrane GTPase.  The bacterial SRPR is called '''FtsY'''.
See also [[Intracellular receptors]]


*<scene name='48/485587/Cv/6'>GTP binding site</scene>. Water molecules are shown as red spheres.
*<scene name='48/485587/Cv/6'>GTP binding site</scene>. Water molecules are shown as red spheres.
*<scene name='48/485587/Cv/7'>Mg coordination site</scene>.
*<scene name='48/485587/Cv/7'>Mg coordination site</scene>.
</StructureSection>
 
==3D structures of signal recognition particle receptor==
==3D structures of signal recognition particle receptor==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[Signal recognition particle receptor 3D structures]]
{{#tree:id=OrganizedByTopic|openlevels=0|


*Signal recognition particle receptor
</StructureSection>  
 
**[[2fh5]] - hSRPR α+β subunits + GTP – human<br />
**[[5l3q]] - hSRPR α subunit + SRP54 + AMP + GNP <br />
**[[2go5]] - hSRPR α subunit + mSRPR β subunit + ribosomal proteins L23, L31, L35 + dSRP19 + dSRP54 + RNA - Cryo EM<br />
**[[1nrj]] – ySRPR α+β subunits + GTP – yeast<br />
**[[2ged]] - ySRPR β subunit (mutant)<br />
 
*Signal recognition particle receptor FtsY
 
**[[3jaj]], [[3jan]] – FtsY in ribosome - rabbit - Cryo EM<br />
**[[5l3r]] – SRPR FtsY + SRP54 - ''Arabidopsis thaliana''<br />
**[[1zu5]], [[1zu4]] – SRPR FtsY NG domain – ''Mycoplasma mycoides''<br />
**[[1vma]] – SRPR FtsY – ''Thermotoga maritima''<br />
**[[6cy1]] – EaSRPR FtsY – ''Elizabethkingia anopheles''<br />
**[[6cy5]] – EaSRPR FtsY NG domain + GDP<br />
**[[2q9a]] – TaSRPR FtsY – ''Thermus aquaticus''<br />
**[[2q9c]], [[2q9b]] – TaSRPR FtsY NG domain + GMPPNP<br />
**[[2j7p]], [[1rj9]], [[1okk]] – TaSRPR FtsY NG domain + signal recognition particle protein <br />
**[[2cnw]] – TaSRPR FtsY NG domain + signal recognition particle protein + GDP<br />
**[[5niy]] – EcSRPR FtsY – ''Escherichia coli''<br />
**[[6fpk]], [[6fpr]] – EcSRPR FtsY N-terminal<br />
**[[2yhs]], [[2qy9]], [[1fts]], [[6cqp]], [[6cs8]], [[6n5i]], [[6n5j]], [[6n6n]], [[6n9b]], [[6nc1]], [[6nc4]] – EcSRPR FtsY NG domain<br />
**[[6fqd]] – EcSRPR FtsY NG domain + GDP<br />
**[[6c58]], [[6cvd]], [[6dlx]] – EcSRPR FtsY NG domain + antibiotic<br />
**[[2iyl]] – EcSRPR FtsY residues 20-303 + GDP<br />
**[[2xxa]] - EcSRPR FtsY NG domain + signal recognition particle protein residues 1-433 (mutant) + 4.5SRNA<br />
**[[3zn8]] - EcSRPR FtsY NG domain + signal recognition particle protein 54 NG domain + 4.5SRNA + dipeptidyl aminopeptidase B<br />
**[[4c7o]] – EcFtsY + EcSRP + SRP RNA<br />
**[[2xkv]] – EcFtsY + EcSRP NG+M domains + 4.5S RNA<br />
**[[5aka]], [[5gad]], [[5nco]], [[5gaf]], [[5gag]], [[5gah]] – EcFtsY in ribosome - Cryo EM<br />
**[[5l3w]] – SRPR FtsY NG domain - ''Sulfolobus acidocaldarius''<br />
**[[5l3s]] – SRPR FtsY + SRP54 + GNP - ''Sulfolobus solfataricus''<br />
**[[3dm9]], [[3dmd]], [[3e70]] – SRPR + GDP – ''Pyrococcus furiosus''
}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman