8S83

Domains 3 and 6 of Sap S-layer protein from Bacillus anthracis

8S83 の概要

• エントリーDOI: 10.2210/pdb8s83/pdb
• 分子名称: S-layer protein sap (3 entities in total)
• 機能のキーワード: s-layer, sap, anthracis, anthrax, structural protein
• 由来する生物種: Bacillus anthracis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47589.41

構造登録者

Sogues, A.,Remaut, H. (登録日: 2024-03-05, 公開日: 2024-11-20, 最終更新日: 2024-12-18)

主引用文献

Sogues, A.,Leigh, K.,Halingstad, E.V.,Van der Verren, S.E.,Cecil, A.J.,Fioravanti, A.,Pak, A.J.,Kudryashev, M.,Remaut, H.
Architecture of the Sap S-layer of Bacillus anthracis revealed by integrative structural biology.
Proc.Natl.Acad.Sci.USA, 121:e2415351121-e2415351121, 2024

PubMed Abstract: is a spore-forming gram-positive bacterium responsible for anthrax, an infectious disease with a high mortality rate and a target of concern due to bioterrorism and long-term site contamination. The entire surface of vegetative cells in exponential or stationary growth phase is covered in proteinaceous arrays called S-layers, composed of Sap or EA1 protein, respectively. The Sap S-layer represents an important virulence factor and cell envelope support structure whose paracrystalline nature is essential for its function. However, the spatial organization of Sap in its lattice state remains elusive. Here, we employed cryoelectron tomography and subtomogram averaging to obtain a map of the Sap S-layer from tubular polymers that revealed a conformational switch between the postassembly protomers and the previously available X-ray structure of the condensed monomers. To build and validate an atomic model of the lattice within this map, we used a combination of molecular dynamics simulations, X-ray crystallography, cross-linking mass spectrometry, and biophysics in an integrative structural biology approach. The Sap lattice model produced recapitulates a close-to-physiological arrangement, reveals high-resolution details of lattice contacts, and sheds light on the mechanisms underlying the stability of the Sap layer.

PubMed: 39652757
DOI: 10.1073/pnas.2415351121

実験手法

X-RAY DIFFRACTION (2.07 Å)