Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family.
Nevskaya, N., Tischenko, S., Fedorov, R., Al-Karadaghi, S., Liljas, A., Kraft, A., Piendl, W., Garber, M., Nikonov, S.(2000) Structure 8: 363-371
- PubMed: 10801481 
- DOI: https://doi.org/10.1016/s0969-2126(00)00116-7
- Primary Citation of Related Structures:  
1CJS - PubMed Abstract: 
L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined.
Organizational Affiliation: 
Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142292, Moscow Region, Russia.