2iyl
From Proteopedia
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| - | [[Image:2iyl.gif|left|200px]]<br /><applet load="2iyl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2iyl, resolution 2.10Å" /> | ||
| - | '''STRUCTURE OF AN FTSY:GDP COMPLEX'''<br /> | ||
| - | == | + | ==Structure of an FtsY:GDP complex== |
| - | + | <StructureSection load='2iyl' size='340' side='right'caption='[[2iyl]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [ | + | <table><tr><td colspan='2'>[[2iyl]] is a 1 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=2IYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYL 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]] 2.1Å</td></tr> |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=2iyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyl OCA], [https://pdbe.org/2iyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyl RCSB], [https://www.ebi.ac.uk/pdbsum/2iyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyl 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). | |
| - | [[ | + | == 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/iy/2iyl_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=2iyl ConSurf]. |
| - | [ | + | <div style="clear:both"></div> |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| + | FtsY and Ffh are structurally similar prokaryotic Signal Recognition Particle GTPases that play an essential role in the Signal Recognition Particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The two GTPases assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex. We report here the 2.1 A X-ray structure of FtsY from T. aquaticus bound to GDP. The structure of the monomeric protein reveals, unexpectedly, canonical binding interactions for GDP. A comparison of the structures of the monomeric and complexed FtsY NG GTPase domain suggests that it undergoes a conformational change similar to that of Ffh NG during the assembly of the symmetric heterodimeric complex. However, in contrast to Ffh, in which the C-terminal helix shifts independently of the other subdomains, the C-terminal helix and N domain of T. aquaticus FtsY together behave as a rigid body during assembly, suggesting distinct mechanisms by which the interactions of the NG domain "module" are regulated in the context of the two SRP GTPases. | ||
| - | + | X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.,Gawronski-Salerno J, Coon JS 5th, Focia PJ, Freymann DM Proteins. 2007 Mar 1;66(4):984-95. PMID:17186523<ref>PMID:17186523</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2iyl" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Signal recognition particle receptor 3D structures|Signal recognition particle receptor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus aquaticus]] | ||
| + | [[Category: Focia PJ]] | ||
| + | [[Category: Freymann DM]] | ||
Current revision
Structure of an FtsY:GDP complex
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