A mutant form of the ribosomal protein L1 reveals conformational flexibility

FEBS Letters

Nikonov, S³  Garber, M³  Eliseikina, I³  Ossina, N³  Al-Karadaghi, S²  Nevskaya, N³  Liljas, A²  Fomenkova, N³  Jonsson, B.-H¹  Unge, J² 

[1] Department of Biochemistry, University of Umeå, S-901 87 Umeå, Sweden;Department of Molecular Biophysics, University of Lund, P.O. Box 124, S-221 00 Lund, Sweden;Department of Structure and Function of Ribosomes, Institute of Protein Research, Russia Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

关键词: Ribosomal protein;    X-ray crystallography;    Conformational change;    RNA binding;    Protein synthesis;   

DOI  :  10.1016/S0014-5793(97)00611-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown