title: Crystal structure of the N-terminal domains of the surface cell antigen 4 of Rickettsia.
abstract: The obligate intracellular, gram-negative bacterium Rickettsia is the causative agent of spotted fevers and typhus in humans. Surface cell antigen (sca) proteins surround these bacteria. We recently reported the co-localization of one of these proteins, sca4, with vinculin in cells at sites of focal adhesions and demonstrated that two vinculin binding sites directed the sca4/vinculin interaction. Here we report the 2.2 Å crystal structure of the conserved N-terminal 38 kDa domain of sca4 from Rickettsia rickettsii. The structure reveals two subdomains. The first is an all-helical domain that is folded in a fashion similar to the dimeric assembly chaperone for rubisco, namely RbcX. The following and highly conserved β-strand domain lacks significant structural similarity with other known structures and to the best of our knowledge represents a new protein fold.
authors.affiliation: Department of Cancer Biology, Cell Adhesion Laboratory, The Scripps Research Institute, Jupiter, Florida, 33458.
authors.forename: Jun Hyuck
authors.initials: JH
authors.lastname: Lee
authors.forename: Clemens
authors.initials: C
authors.lastname: Vonrhein
authors.forename: Gerard
authors.initials: G
authors.lastname: Bricogne
authors.forename: Tina
authors.initials: T
authors.lastname: Izard
mesh_terms: D000954:Antigens, Surface / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D022001:Focal Adhesions / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012284:Rickettsia rickettsii / Q000737:chemistry*; D016596:Vinculin / Q000378:metabolism
chemical_list: D000954:Antigens, Surface; D001426:Bacterial Proteins; D016596:Vinculin
keywords: Rickettsia rickettsia; X-ray crystallography; novel fold; vinculin
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