期刊
STRUCTURE
卷 23, 期 5, 页码 863-872出版社
CELL PRESS
DOI: 10.1016/j.str.2015.03.001
关键词
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资金
- Max Planck Society
- ERC [311523]
- NIH [AI22160, GM105404]
- United States Department of Energy
- European Research Council (ERC) [311523] Funding Source: European Research Council (ERC)
Archaea employ the archaellum, a type IV pilus-like nanomachine, for swimming motility. In the crenarchaeon Sulfolobus acidocaldarius, the archaellum consists of seven proteins: FlaB/X/G/F/H/I/J. FlaF is conserved and essential for archaellum assembly but no FlaF structures exist. Here, we truncated the FlaF N terminus and solved 1.5-angstrom and 1.65-angstrom resolution crystal structures of this monotopic membrane protein. Structures revealed an N-terminal alpha-helix and an eight-strand beta-sandwich, immunoglobulin-like fold with striking similarity to S-layer proteins. Crystal structures, X-ray scattering, and mutational analyses suggest dimer assembly is needed for in vivo function. The sole cell envelope component of S. acidocaldarius is a paracrystalline S-layer, and FlaF specifically bound to S-layer protein, suggesting that its interaction domain is located in the pseudoperiplasm with its N-terminal helix in the membrane. From these data, FlaF may act as the previously unknown archaellum stator protein that anchors the rotating archaellum to the archaeal cell envelope.
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