7PNB

Sulfolobus acidocaldarius 0406 filament.

7PNB の概要

• エントリーDOI: 10.2210/pdb7pnb/pdb
• EMDBエントリー: 13546
• 分子名称: Sulfolobus acidocaldarius 0406 filament., beta-D-glucopyranose-(1-4)-6-deoxy-6-sulfo-beta-D-glucopyranose-(1-3)-[alpha-D-mannopyranose-(1-4)][alpha-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 6-deoxy-6-sulfo-beta-D-glucopyranose-(1-3)-[alpha-D-mannopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: cell surface appendage, beta-strand addition, isopeptide bond, n-glycosylation, beta-sandwich, protein fibril
• 由来する生物種: Sulfolobus acidocaldarius
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 248871.57

構造登録者

Isupov, M.N.,Gaines, M.,Daum, B. (登録日: 2021-09-06, 公開日: 2022-09-14, 最終更新日: 2024-11-06)

主引用文献

Gaines, M.C.,Isupov, M.N.,Sivabalasarma, S.,Haque, R.U.,McLaren, M.,Mollat, C.L.,Tripp, P.,Neuhaus, A.,Gold, V.A.M.,Albers, S.V.,Daum, B.
Electron cryo-microscopy reveals the structure of the archaeal thread filament.
Nat Commun, 13:7411-7411, 2022

PubMed Abstract: Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named "thread". Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism.

PubMed: 36456543
DOI: 10.1038/s41467-022-34652-4

実験手法

ELECTRON MICROSCOPY (3.46 Å)