title: [Crystal structures of mutant ribosomal proteins L1].
abstract: Nine mutant forms of ribosomal proteins L1 from the bacterium Thermus thermophilus and the archaeon Methanococcus jannaschii were obtained. Their crystal structures were determined and analyzed. Earlier determined structure of S179C TthL1 was also thoroughly analyzed. Five from ten mutant proteins reveal essential changes of spatial structure caused by surface point mutation. It proves that for correct studies of biological processes by site-directed mutagenesis it is necessary to determine or at least to model spatial structures of mutant proteins. Detailed comparison of mutant L1 structures with that of corresponding wild type proteins reveals that side chain of a mutated amino acid residue tries to locate like the side chain of the original residue in the wild type protein. This observation helps to model the mutant structures.
authors.forename: E Iu
authors.initials: EIu
authors.lastname: Nikonova
authors.forename: S A
authors.initials: SA
authors.lastname: Volchkov
authors.forename: V G
authors.initials: VG
authors.lastname: Kliashtornyĭ
authors.forename: S V
authors.initials: SV
authors.lastname: Tishchenko
authors.forename: O S
authors.initials: OS
authors.lastname: Kostareva
authors.forename: N A
authors.initials: NA
authors.lastname: Nevskaia
authors.forename: O S
authors.initials: OS
authors.lastname: Nikonov
authors.forename: A G
authors.initials: AG
authors.lastname: Gabdulkhakov
authors.forename: A D
authors.initials: AD
authors.lastname: Nikulin
authors.forename: N L
authors.initials: NL
authors.lastname: Davydova
authors.forename: V A
authors.initials: VA
authors.lastname: Strel'tsov
authors.forename: M B
authors.initials: MB
authors.lastname: Garber
authors.forename: S V
authors.initials: SV
authors.lastname: Nikonov
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D018360:Crystallography, X-Ray; D017017:Methanococcus / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics*; D016963:Thermus thermophilus / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C028546:ribosomal protein L1