1fts: Difference between revisions

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 <StructureSection load='1fts' size='340' side='right'caption='[[1fts]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fts]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FTS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FTS FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fts OCA], [http://pdbe.org/1fts PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fts RCSB], [http://www.ebi.ac.uk/pdbsum/1fts PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fts ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1fts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fts OCA], [https://pdbe.org/1fts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fts RCSB], [https://www.ebi.ac.uk/pdbsum/1fts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fts ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FTSY_ECOLI FTSY_ECOLI]] 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). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.<ref>PMID:8194520</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15148364</ref> <ref>PMID:17682051</ref>
+[https://www.uniprot.org/uniprot/FTSY_ECOLI FTSY_ECOLI] 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). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.<ref>PMID:8194520</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15148364</ref> <ref>PMID:17682051</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fts ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Newly synthesized proteins destined either for secretion or incorporation into membranes are targeted to the membrane translocation machinery by a ubiquitous system consisting of a signal-recognition particle (SRP) and its receptor. Both the SRP receptor and the protein within the SRP that binds the signal sequence contain GTPases. These two proteins, together with the RNA component of the SRP, form a complex and thereby regulate each other's GTPase activity. Here we report the structure of the GTPase-containing portion of FtsY, the functional homologue of the SRP receptor of Escherichia coli, at 2.2 A resolution without bound nucleotide. This so-called NG domain displays similarities to the Ras-related GTPases, as well as features unique to the SRP-type GTPases, such as a separate amino-terminal domain, an insertion within the p21ras (Ras) effector domain, and a wide-open GTP-binding region. The structure explains the low affinity of FtsY for GTP, and suggests rearrangements that may occur on nucleotide binding. It also identifies regions potentially involved in the transmission of signals between domains and in interactions with regulatory proteins.
-Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.,Montoya G, Svensson C, Luirink J, Sinning I Nature. 1997 Jan 23;385(6614):365-8. PMID:9002525<ref>PMID:9002525</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fts" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Signal recognition particle receptor|Signal recognition particle receptor]]
+*[[Signal recognition particle receptor 3D structures|Signal recognition particle receptor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Luirink, J]]
+[[Category: Luirink J]]
-[[Category: Montoya, G]]
+[[Category: Montoya G]]
-[[Category: Sinning, I]]
+[[Category: Sinning I]]
-[[Category: Svensson, C]]
+[[Category: Svensson C]]
-[[Category: Gtpase]]
-[[Category: Protein targeting]]
-[[Category: Signal recognition particle receptor]]