|
|
| (7 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| | |
| ==Structure of the Methanococcus jannaschii ribosome-SecYEBeta channel complex== | | ==Structure of the Methanococcus jannaschii ribosome-SecYEBeta channel complex== |
| <StructureSection load='4v4n' size='340' side='right' caption='[[4v4n]], [[Resolution|resolution]] 9.00Å' scene=''> | | <SX load='4v4n' size='340' side='right' viewer='molstar' caption='[[4v4n]], [[Resolution|resolution]] 9.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4v4n]] is a 69 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j44 3j44]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4N FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4v4n]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vvk 1vvk], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j43 3j43] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j44 3j44]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4N FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j43|3j43]], [[3j44|3j44]], [[1vvk|1vvk]], [[3j21|3j21]], [[3j2l|3j2l]], [[3j20|3j20]]</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]] 9Å</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=4v4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4n RCSB], [http://www.ebi.ac.uk/pdbsum/4v4n 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=4v4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4n OCA], [https://pdbe.org/4v4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4n RCSB], [https://www.ebi.ac.uk/pdbsum/4v4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4n ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [[http://www.uniprot.org/uniprot/SECG_METJA SECG_METJA]] Subunit of the protein translocation channel SecYEG. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. [[http://www.uniprot.org/uniprot/SECE_METJA SECE_METJA]] 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/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.
| |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Many secretory proteins are targeted by signal sequences to a protein-conducting channel, formed by prokaryotic SecY or eukaryotic Sec61 complexes, and are translocated across the membrane during their synthesis. Crystal structures of the inactive channel show that the SecY subunit of the heterotrimeric complex consists of two halves that form an hourglass-shaped pore with a constriction in the middle of the membrane and a lateral gate that faces the lipid phase. The closed channel has an empty cytoplasmic funnel and an extracellular funnel that is filled with a small helical domain, called the plug. During initiation of translocation, a ribosome-nascent chain complex binds to the SecY (or Sec61) complex, resulting in insertion of the nascent chain. However, the mechanism of channel opening during translocation is unclear. Here we have addressed this question by determining structures of inactive and active ribosome-channel complexes with cryo-electron microscopy. Non-translating ribosome-SecY channel complexes derived from Methanocaldococcus jannaschii or Escherichia coli show the channel in its closed state, and indicate that ribosome binding per se causes only minor changes. The structure of an active E. coli ribosome-channel complex demonstrates that the nascent chain opens the channel, causing mostly rigid body movements of the amino- and carboxy-terminal halves of SecY. In this early translocation intermediate, the polypeptide inserts as a loop into the SecY channel with the hydrophobic signal sequence intercalated into the open lateral gate. The nascent chain also forms a loop on the cytoplasmic surface of SecY rather than entering the channel directly.
| |
|
| |
| Structure of the SecY channel during initiation of protein translocation.,Park E, Menetret JF, Gumbart JC, Ludtke SJ, Li W, Whynot A, Rapoport TA, Akey CW Nature. 2013 Oct 23. doi: 10.1038/nature12720. PMID:24153188<ref>PMID:24153188</ref>
| |
|
| |
|
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]] |
| == References == | | *[[Ribosome 3D structures|Ribosome 3D structures]] |
| <references/>
| | *[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| | [[Category: Large Structures]] |
| [[Category: Methanocaldococcus jannaschii]] | | [[Category: Methanocaldococcus jannaschii]] |
| [[Category: Akey, C W]] | | [[Category: Akey CW]] |
| [[Category: Gumbart, J C]] | | [[Category: Gumbart JC]] |
| [[Category: Li, W]] | | [[Category: Li W]] |
| [[Category: Ludtke, S J]] | | [[Category: Ludtke SJ]] |
| [[Category: Menetret, J F]] | | [[Category: Menetret JF]] |
| [[Category: Park, E]] | | [[Category: Park E]] |
| [[Category: Rapoport, T A]] | | [[Category: Rapoport TA]] |
| [[Category: Whynot, A]] | | [[Category: Whynot A]] |
| [[Category: Archaea]]
| |
| [[Category: Archaeal]]
| |
| [[Category: Co-translational translocation]]
| |
| [[Category: Large subunit]]
| |
| [[Category: Protein conducting channel]]
| |
| [[Category: Protein synthesis]]
| |
| [[Category: Ribosomal]]
| |
| [[Category: Ribosome-protein transport complex]]
| |
| [[Category: Rna]]
| |