1rj9

From Proteopedia

(Difference between revisions)

Revision as of 15:26, 27 October 2021

Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)

Structural highlights

1rj9 is a 2 chain structure with sequence from Atcc 25104. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1okk, 1o87, 1ffh, 2ffh, 1ng1, 2ng1, 3ng1, 1ls1, 1jpj, 1jpn, 1duh, 1dul
Gene:	FFH (ATCC 25104)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FTSY_THEAQ] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity). [SRP54_THEAQ] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Signal sequences target proteins for secretion from cells or for integration into cell membranes. As nascent proteins emerge from the ribosome, signal sequences are recognized by the signal recognition particle (SRP), which subsequently associates with its receptor (SR). In this complex, the SRP and SR stimulate each other's GTPase activity, and GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane. To define the mechanism of reciprocal activation, we determined the 1.9 A structure of the complex formed between these two GTPases. The two partners form a quasi-two-fold symmetrical heterodimer. Biochemical analysis supports the importance of the extensive interaction surface. Complex formation aligns the two GTP molecules in a symmetrical, composite active site, and the 3'OH groups are essential for association, reciprocal activation and catalysis. This unique circle of twinned interactions is severed twice on hydrolysis, leading to complex dissociation after cargo delivery.

Substrate twinning activates the signal recognition particle and its receptor.,Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM Nature. 2004 Jan 15;427(6971):215-21. PMID:14724630^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM. Substrate twinning activates the signal recognition particle and its receptor. Nature. 2004 Jan 15;427(6971):215-21. PMID:14724630 doi:10.1038/nature02250

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rj9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rj9' size='340' side='right'caption='[[1rj9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rj9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RJ9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rj9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJ9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1okk|1okk]], [[1o87|1o87]], [[1ffh|1ffh]], [[2ffh|2ffh]], [[1ng1|1ng1]], [[2ng1|2ng1]], [[3ng1|3ng1]], [[1ls1|1ls1]], [[1jpj|1jpj]], [[1jpn|1jpn]], [[1duh|1duh]], [[1dul|1dul]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FFH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FFH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rj9 OCA], [http://pdbe.org/1rj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rj9 RCSB], [http://www.ebi.ac.uk/pdbsum/1rj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rj9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rj9 OCA], [https://pdbe.org/1rj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rj9 RCSB], [https://www.ebi.ac.uk/pdbsum/1rj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rj9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FTSY_THEAQ FTSY_THEAQ]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity). [[http://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]
+[[https://www.uniprot.org/uniprot/FTSY_THEAQ FTSY_THEAQ]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity). [[https://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1rj9

From Proteopedia

Revision as of 15:26, 27 October 2021

Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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