5c78
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==ATP-driven lipid-linked oligosaccharide flippase PglK in apo-inward state (1)== | |
| + | <StructureSection load='5c78' size='340' side='right'caption='[[5c78]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c78]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C78 FirstGlance]. <br> | ||
| + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene></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=5c78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c78 OCA], [https://pdbe.org/5c78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c78 RCSB], [https://www.ebi.ac.uk/pdbsum/5c78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c78 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O86150_CAMJU O86150_CAMJU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The flipping of membrane-embedded lipids containing large, polar head groups is slow and energetically unfavourable, and is therefore catalysed by flippases, the mechanisms of which are unknown. A prominent example of a flipping reaction is the translocation of lipid-linked oligosaccharides that serve as donors in N-linked protein glycosylation. In Campylobacter jejuni, this process is catalysed by the ABC transporter PglK. Here we present a mechanism of PglK-catalysed lipid-linked oligosaccharide flipping based on crystal structures in distinct states, a newly devised in vitro flipping assay, and in vivo studies. PglK can adopt inward- and outward-facing conformations in vitro, but only outward-facing states are required for flipping. While the pyrophosphate-oligosaccharide head group of lipid-linked oligosaccharides enters the translocation cavity and interacts with positively charged side chains, the lipidic polyprenyl tail binds and activates the transporter but remains exposed to the lipid bilayer during the reaction. The proposed mechanism is distinct from the classical alternating-access model applied to other transporters. | ||
| - | + | Structure and mechanism of an active lipid-linked oligosaccharide flippase.,Perez C, Gerber S, Boilevin J, Bucher M, Darbre T, Aebi M, Reymond JL, Locher KP Nature. 2015 Aug 12. doi: 10.1038/nature14953. PMID:26266984<ref>PMID:26266984</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5c78" style="background-color:#fffaf0;"></div> |
| - | [[Category: Locher | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Campylobacter jejuni]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Locher KP]] | ||
| + | [[Category: Perez C]] | ||
Current revision
ATP-driven lipid-linked oligosaccharide flippase PglK in apo-inward state (1)
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