3mp7
From Proteopedia
(Difference between revisions)
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes== | ==Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes== | ||
| - | <StructureSection load='3mp7' size='340' side='right' caption='[[3mp7]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3mp7' size='340' side='right'caption='[[3mp7]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3mp7]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3mp7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MP7 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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=3mp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mp7 OCA], [https://pdbe.org/3mp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mp7 RCSB], [https://www.ebi.ac.uk/pdbsum/3mp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mp7 ProSAT]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [https://www.uniprot.org/uniprot/SECY_PYRFU SECY_PYRFU] 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. Complements an E.coli temperature-sensitive secY mutation; deletion of the last 15 residues prevents complementation, which may indicate a role of this region in translocation.[HAMAP-Rule:MF_01465] | ||
== 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/mp/3mp7_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/3mp7_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/ | + | </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=3mp7 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 23: | Line 25: | ||
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.,Egea PF, Stroud RM Proc Natl Acad Sci U S A. 2010 Sep 20. PMID:20855604<ref>PMID:20855604</ref> | Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.,Egea PF, Stroud RM Proc Natl Acad Sci U S A. 2010 Sep 20. PMID:20855604<ref>PMID:20855604</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 3mp7" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Preprotein translocase|Preprotein translocase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
| - | + | [[Category: Egea PF]] | |
| - | [[Category: Egea | + | [[Category: Stroud RM]] |
| - | [[Category: Stroud | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
| |||||||||||
