title: Review: conformation and folding of novel beta-structural elements in viral fiber proteins: the triple beta-spiral and triple beta-helix.
abstract: Apart from alpha-helical coiled coils and the collagen triple helices, fibrous proteins can contain beta-structure in various conformations. Elongated enzymes such as pectate lyase and the bacteriophage P22 tailspike protein contain single-stranded beta-helices. Virus and bacteriophage fibers, which are often trimeric, have been shown to contain novel triple-stranded beta-structures such as the triple beta-spiral and the triple beta-helix. The conformation and folding of viral fibers containing beta-structure are discussed.
authors.affiliation: Institut de Biologie Structurale (CEA-CNRS-UJF), Grenoble, France. mitraki@ibs.fr
authors.forename: Anna
authors.initials: A
authors.lastname: Mitraki
authors.forename: Stefan
authors.initials: S
authors.lastname: Miller
authors.forename: Mark J
authors.initials: MJ
authors.lastname: van Raaij
mesh_terms: D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000378:metabolism; D001435:Bacteriophages / Q000378:metabolism; D036022:Capsid Proteins / Q000737:chemistry; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D036022:Capsid Proteins; D014764:Viral Proteins; C018315:hexon capsid protein, Adenovirus