Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 08 2021
18 08 2021
Historique:
received:
17
02
2021
accepted:
15
07
2021
entrez:
19
8
2021
pubmed:
20
8
2021
medline:
15
9
2021
Statut:
epublish
Résumé
The endoplasmic reticulum (ER) Hsp70 chaperone BiP is regulated by AMPylation, a reversible inactivating post-translational modification. Both BiP AMPylation and deAMPylation are catalysed by a single ER-localised enzyme, FICD. Here we present crystallographic and solution structures of a deAMPylation Michaelis complex formed between mammalian AMPylated BiP and FICD. The latter, via its tetratricopeptide repeat domain, binds a surface that is specific to ATP-state Hsp70 chaperones, explaining the exquisite selectivity of FICD for BiP's ATP-bound conformation both when AMPylating and deAMPylating Thr518. The eukaryotic deAMPylation mechanism thus revealed, rationalises the role of the conserved Fic domain Glu234 as a gatekeeper residue that both inhibits AMPylation and facilitates hydrolytic deAMPylation catalysed by dimeric FICD. These findings point to a monomerisation-induced increase in Glu234 flexibility as the basis of an oligomeric state-dependent switch between FICD's antagonistic activities, despite a similar mode of engagement of its two substrates - unmodified and AMPylated BiP.
Identifiants
pubmed: 34408154
doi: 10.1038/s41467-021-25076-7
pii: 10.1038/s41467-021-25076-7
pmc: PMC8373988
doi:
Substances chimiques
Endoplasmic Reticulum Chaperone BiP
0
Heat-Shock Proteins
0
Membrane Proteins
0
Adenosine Monophosphate
415SHH325A
Adenosine Triphosphate
8L70Q75FXE
FICD protein, human
EC 2.7.7.-
Nucleotidyltransferases
EC 2.7.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5004Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 200848/Z/16/Z
Pays : United Kingdom
Informations de copyright
© 2021. The Author(s).
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