3jc2
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3jc2 is ON HOLD Authors: Voorhees, R.M., Hegde, R.S. Description: The structure of the mammalian Sec61 channel opened by a signal sequence [[Catego...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The structure of the mammalian Sec61 channel opened by a signal sequence== |
| + | <SX load='3jc2' size='340' side='right' viewer='molstar' caption='[[3jc2]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3jc2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JC2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</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=3jc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jc2 OCA], [https://pdbe.org/3jc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jc2 RCSB], [https://www.ebi.ac.uk/pdbsum/3jc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jc2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/S61A1_CANLF S61A1_CANLF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Secreted and integral membrane proteins compose up to one-third of the biological proteome. These proteins contain hydrophobic signals that direct their translocation across or insertion into the lipid bilayer by the Sec61 protein-conducting channel. The molecular basis of how hydrophobic signals within a nascent polypeptide trigger channel opening is not understood. Here, we used cryo-electron microscopy to determine the structure of an active Sec61 channel that has been opened by a signal sequence. The signal supplants helix 2 of Sec61alpha, which triggers a rotation that opens the central pore both axially across the membrane and laterally toward the lipid bilayer. Comparisons with structures of Sec61 in other states suggest a pathway for how hydrophobic signals engage the channel to gain access to the lipid bilayer. | ||
| - | + | Structure of the Sec61 channel opened by a signal sequence.,Voorhees RM, Hegde RS Science. 2016 Jan 1;351(6268):88-91. doi: 10.1126/science.aad4992. PMID:26721998<ref>PMID:26721998</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 3jc2" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hegde | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Canis lupus familiaris]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hegde RS]] | ||
| + | [[Category: Voorhees RM]] | ||
Current revision
The structure of the mammalian Sec61 channel opened by a signal sequence
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