8QP0

A hexamer pore in the S-layer of Sulfolobus acidocaldarius formed by SlaA protein

This is a non-PDB format compatible entry.

Summary for 8QP0

• Entry DOI: 10.2210/pdb8qp0/pdb
• Related: 7ZCX 8QOX
• EMDB information: 18127
• Descriptor: S-layer protein A (1 entity in total)
• Functional Keywords: s-layer, dimer, n-glycosylation, archea, structural protein
• Biological source: Sulfolobus acidocaldarius DSM 639
• Total number of polymer chains: 6
• Total formula weight: 906470.44

Authors

Gambelli, L.,McLaren, M.,Isupov, M.,Conners, R.,Daum, B. (deposition date: 2023-09-29, release date: 2024-02-21, Last modification date: 2024-11-13)

Primary citation

Gambelli, L.,McLaren, M.,Conners, R.,Sanders, K.,Gaines, M.C.,Clark, L.,Gold, V.A.M.,Kattnig, D.,Sikora, M.,Hanus, C.,Isupov, M.N.,Daum, B.
Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius.
Elife, 13:-, 2024

PubMed Abstract: Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the cell and its environment. Therefore, S-layers are crucial for supporting microbial life. Notwithstanding their importance, little is known about archaeal S-layers at the atomic level. Here, we combined single-particle cryo electron microscopy, cryo electron tomography, and Alphafold2 predictions to generate an atomic model of the two-component S-layer of . The outer component of this S-layer (SlaA) is a flexible, highly glycosylated, and stable protein. Together with the inner and membrane-bound component (SlaB), they assemble into a porous and interwoven lattice. We hypothesise that jackknife-like conformational changes in SlaA play important roles in S-layer assembly.

PubMed: 38251732
DOI: 10.7554/eLife.84617

Experimental method

ELECTRON MICROSCOPY (11.2 Å)