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| | <SX load='6r7l' size='340' side='right' viewer='molstar' caption='[[6r7l]], [[Resolution|resolution]] 6.00Å' scene=''> | | <SX load='6r7l' size='340' side='right' viewer='molstar' caption='[[6r7l]], [[Resolution|resolution]] 6.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6r7l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R7L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6R7L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6r7l]] is a 3 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=6R7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R7L FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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]] 6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6r7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r7l OCA], [http://pdbe.org/6r7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r7l RCSB], [http://www.ebi.ac.uk/pdbsum/6r7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r7l ProSAT]</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=6r7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r7l OCA], [https://pdbe.org/6r7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r7l RCSB], [https://www.ebi.ac.uk/pdbsum/6r7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r7l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SECY_ECOLI SECY_ECOLI]] 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. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.[HAMAP-Rule:MF_01465] | + | [https://www.uniprot.org/uniprot/SECE_ECOLI SECE_ECOLI] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY.<ref>PMID:15140892</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6r7l" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6r7l" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Beckmann R]] |
| - | [[Category: Kater, L]] | + | [[Category: Kater L]] |
| - | [[Category: Kedrov, A]] | + | [[Category: Kedrov A]] |
| - | [[Category: Insertion intermediate]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Monomeric translocon]]
| + | |
| - | [[Category: Nanodisc]]
| + | |
| Structural highlights
Function
SECE_ECOLI Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY.[1]
Publication Abstract from PubMed
The Sec translocon provides the lipid bilayer entry for ribosome-bound nascent chains and thus facilitates membrane protein biogenesis. Despite the appreciated role of the native environment in the translocon:ribosome assembly, structural information on the complex in the lipid membrane is scarce. Here, we present a cryo-electron microscopy-based structure of bacterial translocon SecYEG in lipid nanodiscs and elucidate an early intermediate state upon insertion of the FtsQ anchor domain. Insertion of the short nascent chain causes initial displacements within the lateral gate of the translocon, where alpha-helices 2b, 7, and 8 tilt within the membrane core to "unzip" the gate at the cytoplasmic side. Molecular dynamics simulations demonstrate that the conformational change is reversed in the absence of the ribosome, and suggest that the accessory alpha-helices of SecE subunit modulate the lateral gate conformation. Site-specific cross-linking validates that the FtsQ nascent chain passes the lateral gate upon insertion. The structure and the biochemical data suggest that the partially inserted nascent chain remains highly flexible until it acquires the transmembrane topology.
Partially inserted nascent chain unzips the lateral gate of the Sec translocon.,Kater L, Frieg B, Berninghausen O, Gohlke H, Beckmann R, Kedrov A EMBO Rep. 2019 Aug 5:e48191. doi: 10.15252/embr.201948191. PMID:31379073[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200
- ↑ Kater L, Frieg B, Berninghausen O, Gohlke H, Beckmann R, Kedrov A. Partially inserted nascent chain unzips the lateral gate of the Sec translocon. EMBO Rep. 2019 Aug 5:e48191. doi: 10.15252/embr.201948191. PMID:31379073 doi:http://dx.doi.org/10.15252/embr.201948191
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