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| | <SX load='5abb' size='340' side='right' viewer='molstar' caption='[[5abb]], [[Resolution|resolution]] 8.00Å' scene=''> | | <SX load='5abb' size='340' side='right' viewer='molstar' caption='[[5abb]], [[Resolution|resolution]] 8.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5abb]] 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=5ABB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ABB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5abb]] 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=5ABB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ABB FirstGlance]. <br> |
| - | </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=5abb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abb OCA], [http://pdbe.org/5abb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5abb RCSB], [http://www.ebi.ac.uk/pdbsum/5abb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5abb ProSAT]</span></td></tr> | + | </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=5abb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abb OCA], [https://pdbe.org/5abb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5abb RCSB], [https://www.ebi.ac.uk/pdbsum/5abb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5abb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B7MCR5_ECO45 B7MCR5_ECO45]] 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.[HAMAP-Rule:MF_01465][RuleBase:RU000537] [[http://www.uniprot.org/uniprot/PRRG_PRB01 PRRG_PRB01]] Light-driven proton pump that generates photothrophic energy. [[http://www.uniprot.org/uniprot/B7MIW7_ECO45 B7MIW7_ECO45]] Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.[HAMAP-Rule:MF_00422] | + | [https://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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Beckmann R]] |
| - | [[Category: Berninghausen, O]] | + | [[Category: Berninghausen O]] |
| - | [[Category: Bischoff, L]] | + | [[Category: Bischoff L]] |
| - | [[Category: Wickles, S]] | + | [[Category: Wickles S]] |
| - | [[Category: VanderSluis, E]] | + | [[Category: VanderSluis E]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translocon]]
| + | |
| Structural highlights
Function
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]
Publication Abstract from PubMed
The biogenesis of polytopic membrane proteins occurs co-translationally on ribosomes that are tightly bound to a membrane-embedded protein-conducting channel: the Sec-complex. The path that is followed by nascent proteins inside the ribosome and the Sec-complex is relatively well established; however, it is not clear what the fate of the N-terminal transmembrane domains (TMDs) of polytopic membrane proteins is when the C-terminal TMDs domains are not yet synthesized. Here, we present the sub-nanometer cryo-electron microscopy structure of an in vivo generated ribosome-SecY complex that carries a membrane insertion intermediate of proteorhodopsin (PR). The structure reveals a pre-opened Sec-complex and the first two TMDs of PR already outside the SecY complex directly in front of its proposed lateral gate. Thus, our structure is in agreement with positioning of N-terminal TMDs at the periphery of SecY, and in addition, it provides clues for the molecular mechanism underlying membrane protein topogenesis.
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion.,Bischoff L, Wickles S, Berninghausen O, van der Sluis EO, Beckmann R Nat Commun. 2014 Jun 10;5:4103. doi: 10.1038/ncomms5103. PMID:24912953[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bischoff L, Wickles S, Berninghausen O, van der Sluis EO, Beckmann R. Visualization of a polytopic membrane protein during SecY-mediated membrane insertion. Nat Commun. 2014 Jun 10;5:4103. doi: 10.1038/ncomms5103. PMID:24912953 doi:http://dx.doi.org/10.1038/ncomms5103
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