5nbd: Difference between revisions
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==PglK flippase in complex with inhibitory nanobody== | |||
<StructureSection load='5nbd' size='340' side='right' caption='[[5nbd]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nbd]] is a 3 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBD 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></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=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> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5nbd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Locher, K P]] | |||
[[Category: Pardon, E]] | |||
[[Category: Perez, C]] | [[Category: Perez, C]] | ||
[[Category: Steyaert, J]] | [[Category: Steyaert, J]] | ||
[[Category: | [[Category: Abc transporter flippase]] | ||
[[Category: Nanobody]] | |||
[[Category: Transport protein]] | |||
