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TitleStructural basis of antimicrobial membrane coat assembly by human GBP1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 1, Page 172-184, Year 2025
Publish dateOct 11, 2024
AuthorsTanja Kuhm / Clémence Taisne / Cecilia de Agrela Pinto / Luca Gross / Evdokia A Giannopoulou / Stefan T Huber / Els Pardon / Jan Steyaert / Sander J Tans / Arjen J Jakobi /
PubMed AbstractGuanylate-binding proteins (GBPs) are interferon-inducible guanosine triphosphate hydrolases (GTPases) mediating host defense against intracellular pathogens. Their antimicrobial activity hinges on ...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 GBP1 dimer in its guanine nucleotide-bound state and describe the molecular ultrastructure of the GBP1 coat on liposomes and bacterial lipopolysaccharide membranes. Conformational changes of the middle and GTPase effector domains expose the isoprenylated C terminus for membrane association. The α-helical middle domains form a parallel, crossover arrangement essential for coat formation and position the extended effector domain for intercalation into the lipopolysaccharide layer of gram-negative membranes. Nucleotide binding and hydrolysis create oligomeric scaffolds with contractile abilities that promote membrane extrusion and fragmentation. Our data offer a structural and mechanistic framework for understanding GBP1 effector functions in intracellular immunity.
External linksNat Struct Mol Biol / PubMed:39394410 / PubMed Central
MethodsEM (single particle) / EM (tomography)
Resolution3.7 Å
Structure data

16794

8cqb

EMDB-16794, PDB-8cqb:
Cryo-EM structure of the human GBP1 dimer bound to GDP-AlF3
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-16813: Tomogram of GBP1 coatomers assembled on brain polar lipid-derived small unilamellar vesicles.
Method: EM (tomography)

EMDB-16814: Tomogram of GBP1 coatomers assembled on brain polar lipid-derived small unilamellar vesicles.
Method: EM (tomography)

EMDB-16815: Tomogram of GBP1 coatomers assembled on brain polar lipid-derived small unilamellar vesicles.
Method: EM (tomography)

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Cell-autonomous immunity / intracellular pathogens / GTPase

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