The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Cryo-EM structure of the gasdermin A3 membrane pore
Open accessAbstract
Gasdermins mediate inflammatory cell death after cleavage by caspases or other, unknown enzymes. The cleaved N-terminal fragments bind to acidic membrane lipids to form pores, but the mechanism of pore formation remains unresolved. Here we present the cryo-electron microscopy structures of the 27-fold and 28-fold single-ring pores formed by the N-terminal fragment of mouse GSDMA3 (GSDMA3-NT) at 3.8 and 4.2 Å resolutions, and of a double-ring pore at 4.6 Å resolution. In the 27-fold pore, a 108-stranded anti-parallel β-barrel is formed by two β-hairpins from each subunit capped by a globular domain. We identify a positively charged helix that interacts with the acidic lipid cardiolipin. GSDMA3-NT undergoes radical conformational changes upon membrane insertion to form long, membrane-spanning β-strands. We also observe an unexpected additional symmetric ring of GSDMA3-NT subunits that does not insert into the membrane in the double-ring pore, which may represent a pre-pore state of GSDMA3-NT. These structures provide a basis that explains the activities of several mutant gasdermins, including defective mutants that are associated with cancer. High-resolution cryo-electron microscopy structures of the membrane-pore-forming domain of the mouse gasdermin GSDMA3 show that it forms pores with 26-, 27- or 28-fold symmetry and indicate that it may also form a parallel, soluble, pre-pore ring structure.
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Metadata
- Authors
- Ruan, J., Xia, S., Liu, X., Lieberman, J., & Wu, H.
- Venue
- Nature
- Published
- 2018-04-25
- Volume
- 557
- Issue
- 7703
- Pages
- 62-67
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2802099741
- Cited by
- 389
- References
- 31
- FWCI
- 13.11
- Type
- journal article
- Language
- en
- Open access
- green
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