3bo0: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==Ribosome-SecY complex==
-<StructureSection load='3bo0' size='340' side='right' caption='[[3bo0]], [[Resolution|resolution]] 9.60&Aring;' scene=''>
+<SX load='3bo0' size='340' side='right' viewer='molstar' caption='[[3bo0]], [[Resolution|resolution]] 9.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3bo0]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BO0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3bo0]] is a 7 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=3BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BO0 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bo1|3bo1]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.6&#8491;</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=3bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bo0 OCA], [http://pdbe.org/3bo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bo0 RCSB], [http://www.ebi.ac.uk/pdbsum/3bo0 PDBsum]</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=3bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bo0 OCA], [https://pdbe.org/3bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/3bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bo0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SECY_METJA SECY_METJA] The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
 == 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/bo/3bo0_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3bo0_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 16: / Line 19: @@
 </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=3bo0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The SecY complex associates with the ribosome to form a protein translocation channel in the bacterial plasma membrane. We have used cryo-electron microscopy and quantitative mass spectrometry to show that a nontranslating E. coli ribosome binds to a single SecY complex. The crystal structure of an archaeal SecY complex was then docked into the electron density maps. In the resulting model, two cytoplasmic loops of SecY extend into the exit tunnel near proteins L23, L29, and L24. The loop between transmembrane helices 8 and 9 interacts with helices H59 and H50 in the large subunit RNA, while the 6/7 loop interacts with H7. We also show that point mutations of basic residues within either loop abolish ribosome binding. We suggest that SecY binds to this primary site on the ribosome and subsequently captures and translocates the nascent chain.
-Ribosome binding of a single copy of the SecY complex: implications for protein translocation.,Menetret JF, Schaletzky J, Clemons WM Jr, Osborne AR, Skanland SS, Denison C, Gygi SP, Kirkpatrick DS, Park E, Ludtke SJ, Rapoport TA, Akey CW Mol Cell. 2007 Dec 28;28(6):1083-92. PMID:18158904<ref>PMID:18158904</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3bo0" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Preprotein translocase|Preprotein translocase]]
+*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
-== References ==
-<references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Escherichia coli]]
-[[Category: Akey, C W]]
+[[Category: Large Structures]]
-[[Category: Menetret, J F]]
+[[Category: Akey CW]]
-[[Category: Protein translocation]]
+[[Category: Menetret JF]]
-[[Category: Ribosome]]
-[[Category: Ribosome-secy complex]]