Cryo-EM structure of the human GBP1 dimer bound to GDP-AlF3
Ontology highlight
ABSTRACT:
SUBMITTER: Arjen J Jakobi
PROVIDER: EMPIAR-11459 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis of antimicrobial membrane coat assembly by human GBP1.
Kuhm Tanja T Taisne Clémence C de Agrela Pinto Cecilia C Gross Luca L Giannopoulou Evdokia A EA Huber Stefan T ST Pardon Els E Steyaert Jan J Tans Sander J SJ Jakobi Arjen J AJ
Nature structural & molecular biology 20241011 1
Guanylate-binding proteins (GBPs) are interferon-inducible guanosine triphosphate hydrolases (GTPases) mediating host defense against intracellular pathogens. Their antimicrobial activity hinges on their ability to self-associate and coat pathogen-associated compartments or cytosolic bacteria. Coat formation depends on GTPase activity but how nucleotide binding and hydrolysis prime coat formation remains unclear. Here, we report the cryo-electron microscopy structure of the full-length human GBP ...[more]
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