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| | <StructureSection load='6hrc' size='340' side='right'caption='[[6hrc]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='6hrc' size='340' side='right'caption='[[6hrc]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hrc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HRC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HRC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hrc]] 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=6HRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HRC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nbd|5nbd]], [[5c73|5c73]], [[5c76|5c76]], [[5c78|5c78]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wlaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</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=6hrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hrc OCA], [https://pdbe.org/6hrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hrc RCSB], [https://www.ebi.ac.uk/pdbsum/6hrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hrc ProSAT]</span></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=6hrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hrc OCA], [http://pdbe.org/6hrc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hrc RCSB], [http://www.ebi.ac.uk/pdbsum/6hrc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hrc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O86150_CAMJU O86150_CAMJU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter fetus subsp. jejuni smibert 1974]] | + | [[Category: Campylobacter jejuni]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Locher, K P]] | + | [[Category: Locher KP]] |
| - | [[Category: Perez, C]] | + | [[Category: Perez C]] |
| - | [[Category: Abc transporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
O86150_CAMJU
Publication Abstract from PubMed
PglK is a lipid-linked oligosaccharide (LLO) flippase essential for asparagine-linked protein glycosylation in Campylobacter jejuni. Previously we have proposed a non-alternating-access LLO translocation mechanism, where postulated outward-facing states play a primary role. To investigate this unusual mechanistic proposal, we have determined a high-resolution structure of PglK that displays an outward semi-occluded state with the two nucleotide binding domains forming an asymmetric closed dimer with two bound ATPgammaS molecules. Based on this structure, we performed extensive molecular dynamics simulations to investigate LLO recognition and flipping. Our results suggest that PglK may employ a "substrate-hunting" mechanism to locally increase the LLO concentration and facilitate its jump into the translocation pathway, for which sugars from the LLO head group are essential. We further conclude that the release of LLO to the outside occurs before ATP hydrolysis and is followed by the closing of the periplasmic cavity of PglK.
Structure of Outward-Facing PglK and Molecular Dynamics of Lipid-Linked Oligosaccharide Recognition and Translocation.,Perez C, Mehdipour AR, Hummer G, Locher KP Structure. 2019 Feb 8. pii: S0969-2126(19)30013-9. doi:, 10.1016/j.str.2019.01.013. PMID:30799077[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Perez C, Mehdipour AR, Hummer G, Locher KP. Structure of Outward-Facing PglK and Molecular Dynamics of Lipid-Linked Oligosaccharide Recognition and Translocation. Structure. 2019 Feb 8. pii: S0969-2126(19)30013-9. doi:, 10.1016/j.str.2019.01.013. PMID:30799077 doi:http://dx.doi.org/10.1016/j.str.2019.01.013
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