title: Domain movements of HAP2 in the cap-filament complex formation and growth process of the bacterial flagellum.
abstract: The cap at the growing end of the bacterial flagellum is essential for its growth, remaining stably attached while permitting the insertion of flagellin transported from the cytoplasm through the narrow central channel. We analyzed the structure of the isolated cap in its frozen hydrated state by electron cryomicroscopy. The 3D density map now shows detailed features of domains and their connections, giving reliable volumes and masses, making assignment of the domains to the amino acid sequence possible. A model of the cap-filament complex built with an atomic model of the filament allows a quantitative analysis of the cap domain movements on cap binding and rotation that promotes the efficient self assembly of flagellin during the filament growth process.
authors.affiliation: Protonic NanoMachine Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 3-4 Hikaridai, Seika, Kyoto 619-0237, Japan.
authors.forename: Saori
authors.initials: S
authors.lastname: Maki-Yonekura
authors.forename: Koji
authors.initials: K
authors.lastname: Yonekura
authors.forename: Keiichi
authors.initials: K
authors.lastname: Namba
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D004926:Escherichia coli / Q000502:physiology* / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D005407:Flagella / Q000502:physiology*; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D012475:Salmonella / Q000502:physiology / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C076733:FlaD protein, Bacteria