title: FlaX, a unique component of the crenarchaeal archaellum, forms oligomeric ring-shaped structures and interacts with the motor ATPase FlaI.
abstract: Archaella are the archaeal motility structure, which are structurally similar to gram-negative bacterial type IV pili but functionally resemble bacterial flagella. Structural and biochemical data of archaellum subunits are missing. FlaX, a conserved subunit in crenarchaeal archaella, formed high molecular weight complexes that adapted a ring-like structure with an approximate diameter of 30 nm. The C terminus of FlaX was not only involved in the oligomerization, but also essential for FlaX interaction with FlaI, the bifunctional ATPase that is involved in assembly and rotation of the archaellum. This study gives first insights in the assembly apparatus of archaella.
authors.affiliation: Department of Molecular Biology of Archaea, Max Planck Institute for terrestrial Microbiology, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany.
authors.forename: Ankan
authors.initials: A
authors.lastname: Banerjee
authors.forename: Abhrajyoti
authors.initials: A
authors.lastname: Ghosh
authors.forename: Deryck J
authors.initials: DJ
authors.lastname: Mills
authors.forename: Jörg
authors.initials: J
authors.lastname: Kahnt
authors.forename: Janet
authors.initials: J
authors.lastname: Vonck
authors.forename: Sonja-Verena
authors.initials: SV
authors.lastname: Albers
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D016945:Sulfolobus acidocaldarius / Q000235:genetics / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D046912:Multiprotein Complexes; D000251:Adenosine Triphosphatases