2ffh: Difference between revisions

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-[[Image:2ffh.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2ffh", creates the "Structure Box" on the page.
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-{{STRUCTURE_2ffh|  PDB=2ffh  |  SCENE=  }}
-'''THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS'''
+==THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS==
+<StructureSection load='2ffh' size='340' side='right'caption='[[2ffh]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ffh]] is a 3 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=2FFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FFH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ffh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ffh OCA], [https://pdbe.org/2ffh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ffh RCSB], [https://www.ebi.ac.uk/pdbsum/2ffh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ffh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/2ffh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2ffh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues. The groove defines a flexible, hydrophobic environment that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of different lengths and amino acid sequence. The structure also reveals a helix-turn-helix motif containing an arginine-rich alpha helix that is required for binding to SRP RNA and is implicated in forming the core of an extended RNA binding surface.
-==Overview==
+Crystal structure of the signal sequence binding subunit of the signal recognition particle.,Keenan RJ, Freymann DM, Walter P, Stroud RM Cell. 1998 Jul 24;94(2):181-91. PMID:9695947<ref>PMID:9695947</ref>
-The crystal structure of the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues. The groove defines a flexible, hydrophobic environment that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of different lengths and amino acid sequence. The structure also reveals a helix-turn-helix motif containing an arginine-rich alpha helix that is required for binding to SRP RNA and is implicated in forming the core of an extended RNA binding surface.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-FFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFH OCA].
+</div>
+<div class="pdbe-citations 2ffh" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of the signal sequence binding subunit of the signal recognition particle., Keenan RJ, Freymann DM, Walter P, Stroud RM, Cell. 1998 Jul 24;94(2):181-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9695947 9695947]
+*[[Signal recognition particle protein|Signal recognition particle protein]]
-[[Category: Single protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermus aquaticus]]
-[[Category: Freymann, D M.]]
+[[Category: Freymann DM]]
-[[Category: Keenan, R J.]]
+[[Category: Keenan RJ]]
-[[Category: Stroud, R M.]]
+[[Category: Stroud RM]]
-[[Category: Walter, P.]]
+[[Category: Walter P]]
-[[Category: Ffh]]
-[[Category: Gtpase]]
-[[Category: Helix-turn-helix]]
-[[Category: M domain]]
-[[Category: Protein targeting]]
-[[Category: Rna-binding]]
-[[Category: Signal recognition particle]]
-[[Category: Signal sequence-binding]]
-[[Category: Srp54]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:49:56 2008''