title: Structure of the L1 protuberance in the ribosome.
abstract: The L1 protuberance of the 50S ribosomal subunit is implicated in the release/disposal of deacylated tRNA from the E site. The apparent mobility of this ribosomal region has thus far prevented an accurate determination of its three-dimensional structure within either the 50S subunit or the 70S ribosome. Here we report the crystal structure at 2.65 A resolution of ribosomal protein L1 from Sulfolobus acidocaldarius in complex with a specific 55-nucleotide fragment of 23S rRNA from Thermus thermophilus. This structure fills a major gap in current models of the 50S ribosomal subunit. The conformations of L1 and of the rRNA fragment differ dramatically from those within the crystallographic model of the T. thermophilus 70S ribosome. Incorporation of the L1-rRNA complex into the structural models of the T. thermophilus 70S ribosome and the Deinococcus radiodurans 50S subunit gives a reliable representation of most of the L1 protuberance within the ribosome.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
authors.forename: Alexei
authors.initials: A
authors.lastname: Nikulin
authors.forename: Irina
authors.initials: I
authors.lastname: Eliseikina
authors.forename: Svetlana
authors.initials: S
authors.lastname: Tishchenko
authors.forename: Natalia
authors.initials: N
authors.lastname: Nevskaya
authors.forename: Natalia
authors.initials: N
authors.lastname: Davydova
authors.forename: Olga
authors.initials: O
authors.lastname: Platonova
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Piendl
authors.forename: Maria
authors.initials: M
authors.lastname: Selmer
authors.forename: Anders
authors.initials: A
authors.lastname: Liljas
authors.forename: Denis
authors.initials: D
authors.lastname: Drygin
authors.forename: Robert
authors.initials: R
authors.lastname: Zimmermann
authors.forename: Maria
authors.initials: M
authors.lastname: Garber
authors.forename: Stanislav
authors.initials: S
authors.lastname: Nikonov
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D001483:Base Sequence; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D019642:RNA, Archaeal / Q000737:chemistry / Q000235:genetics; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics; D012338:RNA, Ribosomal, 23S / Q000737:chemistry / Q000235:genetics; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics; D012270:Ribosomes / Q000737:chemistry*; D016945:Sulfolobus acidocaldarius / Q000737:chemistry / Q000235:genetics; D016963:Thermus thermophilus / Q000737:chemistry / Q000235:genetics
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D046911:Macromolecular Substances; D019642:RNA, Archaeal; D012329:RNA, Bacterial; D012338:RNA, Ribosomal, 23S; D012269:Ribosomal Proteins; C028546:ribosomal protein L1