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==Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase==
==Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase==
<StructureSection load='3din' size='340' side='right' caption='[[3din]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
<StructureSection load='3din' size='340' side='right'caption='[[3din]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3din]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8] and [http://en.wikipedia.org/wiki/Thermotoga_sp. Thermotoga sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DIN FirstGlance]. <br>
<table><tr><td colspan='2'>[[3din]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8] and [https://en.wikipedia.org/wiki/Thermotoga_sp._RQ2 Thermotoga sp. RQ2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 4.5&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secA, TM_1578 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8]), secY, TM_1480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8]), secE, TM_0452 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8]), secG, TRQ2_0456 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28240 Thermotoga sp.])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3din OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3din RCSB], [http://www.ebi.ac.uk/pdbsum/3din 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=3din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3din OCA], [https://pdbe.org/3din PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3din RCSB], [https://www.ebi.ac.uk/pdbsum/3din PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3din ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SECA_THEMA SECA_THEMA]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity). [[http://www.uniprot.org/uniprot/SECE_THEMA SECE_THEMA]] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. [[http://www.uniprot.org/uniprot/Q9X1I9_THEMA Q9X1I9_THEMA]] 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.  
[https://www.uniprot.org/uniprot/SECE_THEMA SECE_THEMA] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/3din_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/3din_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3din ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3din" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Preprotein translocase|Preprotein translocase]]
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
*[[SecA|SecA]]
*[[SecA|SecA]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thermotoga maritima msb8]]
[[Category: Large Structures]]
[[Category: Thermotoga sp]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Nam, Y]]
[[Category: Thermotoga sp. RQ2]]
[[Category: Rapoport, T A]]
[[Category: Nam Y]]
[[Category: Zimmer, J]]
[[Category: Rapoport TA]]
[[Category: Atp-binding]]
[[Category: Zimmer J]]
[[Category: Atpase]]
[[Category: Inner membrane]]
[[Category: Membrane protein]]
[[Category: Nucleotide-binding]]
[[Category: Protein translocation]]
[[Category: Protein transport]]
[[Category: Transmembrane]]
[[Category: Transport]]

Latest revision as of 09:05, 13 August 2026

Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase

3din, resolution 4.50Å

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