5eul
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the SecA-SecY complex with a translocating polypeptide substrate== | |
| - | + | <StructureSection load='5eul' size='340' side='right' caption='[[5eul]], [[Resolution|resolution]] 3.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5eul]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EUL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TBR:HEXATANTALUM+DODECABROMIDE'>TBR</scene></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=5eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eul OCA], [http://pdbe.org/5eul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eul RCSB], [http://www.ebi.ac.uk/pdbsum/5eul PDBsum]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/SECA_BACSU SECA_BACSU]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382] [[http://www.uniprot.org/uniprot/A4IJK8_GEOTN A4IJK8_GEOTN]] 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] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ingram, J]] | [[Category: Ingram, J]] | ||
[[Category: Li, L]] | [[Category: Li, L]] | ||
| - | [[Category: | + | [[Category: Ling, J]] |
[[Category: Park, E]] | [[Category: Park, E]] | ||
| + | [[Category: Ploegh, H]] | ||
| + | [[Category: Rapoport, T A]] | ||
| + | [[Category: Atpase]] | ||
| + | [[Category: Channel]] | ||
| + | [[Category: Protein transport]] | ||
| + | [[Category: Seca]] | ||
| + | [[Category: Secy]] | ||
Revision as of 03:56, 10 March 2016
Structure of the SecA-SecY complex with a translocating polypeptide substrate
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Categories: Ingram, J | Li, L | Ling, J | Park, E | Ploegh, H | Rapoport, T A | Atpase | Channel | Protein transport | Seca | Secy
