View source for 5nbd


==PglK flippase in complex with inhibitory nanobody==
<StructureSection load='5nbd' size='340' side='right'caption='[[5nbd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9&#8491;</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'>[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>
== 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;">
== 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<ref>PMID:28422165</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nbd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Locher KP]]
[[Category: Pardon E]]
[[Category: Perez C]]
[[Category: Steyaert J]]