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A mutant form of the ribosomal protein L1 reveals conformational flexibility
Author(s) -
Unge J,
Al-Karadaghi S,
Liljas A,
Jonsson B.-H,
Eliseikina I,
Ossi,
Nevskaya N,
Fomenkova N,
Garber M,
Nikonov S
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00611-x
Subject(s) - thermus thermophilus , mutant , conformational change , ribosomal protein , chemistry , biophysics , crystallography , ribosome , rna , biology , microbiology and biotechnology , biochemistry , escherichia coli , gene
The crystal structure of the mutant S179C of the ribosomal protein L1 from Thermus thermophilus has been determined at 1.9 Å resolution. The mutant molecule displays a small but significant opening of the cavity between the two domains. The domain movement seems to be facilitated by the flexibility of at least two conserved glycines. These glycines may be necessary for the larger conformational change needed for an induced fit mechanism upon binding RNA. The domain movement makes a disulfide bridge possible between the incorporated cysteines in two monomers of the mutant L1.