2q9c: Difference between revisions

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 <StructureSection load='2q9c' size='340' side='right'caption='[[2q9c]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2q9c]] 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=2Q9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q9C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2q9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q9C FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2q9a|2q9a]], [[2q9b|2q9b]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsY ([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'>[https://proteopedia.org/fgij/fg.htm?mol=2q9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9c OCA], [https://pdbe.org/2q9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q9c RCSB], [https://www.ebi.ac.uk/pdbsum/2q9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9c ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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/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).
 == 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=2q9c ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The signal recognition particle (SRP) and its conjugate receptor (SR) mediate cotranslational targeting of a subclass of proteins destined for secretion to the endoplasmic reticulum membrane in eukaryotes or to the plasma membrane in prokaryotes. Conserved active site residues in the GTPase domains of both SRP and SR mediate discrete conformational changes during formation and dissociation of the SRP.SR complex. Here, we describe structures of the prokaryotic SR, FtsY, as an apo protein and in two different complexes with a non-hydrolysable GTP analog (GMPPNP). These structures reveal intermediate conformations of FtsY containing GMPPNP and explain how the conserved active site residues position the nucleotide into a non-catalytic conformation. The basis for the lower specificity of binding of nucleotide in FtsY prior to heterodimerization with the SRP conjugate Ffh is also shown. We propose that these structural changes represent discrete conformational states assumed by FtsY during targeting complex formation and dissociation.
-X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.,Reyes CL, Rutenber E, Walter P, Stroud RM PLoS ONE. 2007 Jul 11;2(7):e607. PMID:17622352<ref>PMID:17622352</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2q9c" 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: Atcc 25104]]
 [[Category: Large Structures]]
-[[Category: Reyes, C L]]
+[[Category: Thermus aquaticus]]
-[[Category: Stroud, R M]]
+[[Category: Reyes CL]]
-[[Category: Cell cycle]]
+[[Category: Stroud RM]]
-[[Category: Cell division]]
-[[Category: Ffh]]
-[[Category: Ftsy]]
-[[Category: Gdp]]
-[[Category: Gtp-binding]]
-[[Category: Gtpase]]
-[[Category: Inner membrane]]
-[[Category: Membrane]]
-[[Category: Nucleotide-binding]]
-[[Category: Ribonucleoprotein]]
-[[Category: Rna-binding]]
-[[Category: Signal recognition particle]]
-[[Category: Signaling protein]]
-[[Category: Srp]]