Structural basis for selective AMPylation of Rac-subfamily GTPases by
AMPylation
Bartonella effector protein
FIC domain
RhoGTPases
structure function
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
23 03 2021
23 03 2021
Historique:
entrez:
16
3
2021
pubmed:
17
3
2021
medline:
7
9
2021
Statut:
ppublish
Résumé
Small GTPases of the Ras-homology (Rho) family are conserved molecular switches that control fundamental cellular activities in eukaryotic cells. As such, they are targeted by numerous bacterial toxins and effector proteins, which have been intensively investigated regarding their biochemical activities and discrete target spectra; however, the molecular mechanism of target selectivity has remained largely elusive. Here we report a bacterial effector protein that selectively targets members of the Rac subfamily in the Rho family of small GTPases but none in the closely related Cdc42 or RhoA subfamilies. This exquisite target selectivity of the FIC domain AMP-transferase Bep1 from
Identifiants
pubmed: 33723071
pii: 2023245118
doi: 10.1073/pnas.2023245118
pmc: PMC8000347
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Membrane Proteins
0
rac GTP-Binding Proteins
EC 3.6.5.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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