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| <StructureSection load='5nbd' size='340' side='right'caption='[[5nbd]], [[Resolution|resolution]] 3.90Å' scene=''> | | <StructureSection load='5nbd' size='340' side='right'caption='[[5nbd]], [[Resolution|resolution]] 3.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5nbd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974] and [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NBD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nbd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NBD FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 3.9Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbd OCA], [http://pdbe.org/5nbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbd RCSB], [http://www.ebi.ac.uk/pdbsum/5nbd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbd ProSAT]</span></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=5nbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbd OCA], [https://pdbe.org/5nbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nbd RCSB], [https://www.ebi.ac.uk/pdbsum/5nbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbd ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/PGLK_CAMJE PGLK_CAMJE] Mediates the translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate into the periplasm during the N-linked protein glycosylation pathway.<ref>PMID:16498400</ref> <ref>PMID:16547029</ref> |
| <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: Camelus glama]] | + | [[Category: Lama glama]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Locher, K P]] | + | [[Category: Locher KP]] |
- | [[Category: Pardon, E]] | + | [[Category: Pardon E]] |
- | [[Category: Perez, C]] | + | [[Category: Perez C]] |
- | [[Category: Steyaert, J]] | + | [[Category: Steyaert J]] |
- | [[Category: Abc transporter flippase]]
| + | |
- | [[Category: Nanobody]]
| + | |
- | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
PGLK_CAMJE Mediates the translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate into the periplasm during the N-linked protein glycosylation pathway.[1] [2]
Publication Abstract from PubMed
PglK is an ABC transporter that flips a lipid-linked oligosaccharide (LLO) that serves as a donor in protein N-glycosylation. Previous structures revealed two inward-facing conformations, both with very large separations of the nucleotide binding domains (NBDs), and a closed, ADP-bound state that featured an occluded cavity. To investigate additional states, we developed conformation-sensitive, single-domain camelid nanobodies (Nb) and studied their effect on PglK activity. Biochemical, structural, and mass spectrometric analyses revealed that one inhibitory Nb binds as a single copy to homodimeric PglK. The co-crystal structure of this Nb and ADP-bound PglK revealed a new, narrowly inward-open conformation. Rather than inducing asymmetry in the PglK homodimer, the binding of one Nb results in steric constraints that prevent a second Nb to access the symmetry-related site in PglK. The Nb performed its inhibitory role by a "sticky-doorstop" mechanism, where inhibition of ATP hydrolysis and LLO flipping activity occurs due to impaired closing of the NBD interface, which prevents PglK from converting to an outward-open conformation. This inhibitory mode suggests tight conformational coupling between the ATPase sites, which may apply to other ABC transporters.
Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody.,Perez C, Kohler M, Janser D, Pardon E, Steyaert J, Zenobi R, Locher KP Sci Rep. 2017 Apr 19;7:46641. doi: 10.1038/srep46641. PMID:28422165[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alaimo C, Catrein I, Morf L, Marolda CL, Callewaert N, Valvano MA, Feldman MF, Aebi M. Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides. EMBO J. 2006 Mar 8;25(5):967-76. Epub 2006 Feb 23. PMID:16498400 doi:http://dx.doi.org/10.1038/sj.emboj.7601024
- ↑ Kelly J, Jarrell H, Millar L, Tessier L, Fiori LM, Lau PC, Allan B, Szymanski CM. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J Bacteriol. 2006 Apr;188(7):2427-34. PMID:16547029 doi:http://dx.doi.org/10.1128/JB.188.7.2427-2434.2006
- ↑ Perez C, Kohler M, Janser D, Pardon E, Steyaert J, Zenobi R, Locher KP. Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody. Sci Rep. 2017 Apr 19;7:46641. doi: 10.1038/srep46641. PMID:28422165 doi:http://dx.doi.org/10.1038/srep46641
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