title: Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX.
abstract: The ComX pheromone is an extracellular signaling molecule that stimulates natural competence in response to crowding in the gram-positive bacterium Bacillus subtilis. The pheromone is formed by isoprenylation of an inactive precursor peptide, but its precise structure is not known. Here we report the structure of the ComX pheromone, showing that addition of a geranyl group to a tryptophan residue results in the formation of an unusual ring structure.
authors.affiliation: Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Okada
authors.forename: Isao
authors.initials: I
authors.lastname: Sato
authors.forename: Soo Jeong
authors.initials: SJ
authors.lastname: Cho
authors.forename: Hidehisa
authors.initials: H
authors.lastname: Iwata
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Nishio
authors.forename: David
authors.initials: D
authors.lastname: Dubnau
authors.forename: Youji
authors.initials: Y
authors.lastname: Sakagami
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry*; D008969:Molecular Sequence Data; D010675:Pheromones / Q000096:biosynthesis / Q000737:chemistry*; D011487:Protein Conformation; D014364:Tryptophan / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; C087040:ComX protein, Bacillus subtilis; D010675:Pheromones; D014364:Tryptophan