Structural highlights
Function
[RL1_THETH] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the mutant S179C of the ribosomal protein L1 from Thermus thermophilus has been determined at 1.9 A 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.
A mutant form of the ribosomal protein L1 reveals conformational flexibility.,Unge J, Al-Karadaghi S, Liljas A, Jonsson BH, Eliseikina I, Ossina N, Nevskaya N, Fomenkova N, Garber M, Nikonov S FEBS Lett. 1997 Jul 7;411(1):53-9. PMID:9247141[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Unge J, Al-Karadaghi S, Liljas A, Jonsson BH, Eliseikina I, Ossina N, Nevskaya N, Fomenkova N, Garber M, Nikonov S. A mutant form of the ribosomal protein L1 reveals conformational flexibility. FEBS Lett. 1997 Jul 7;411(1):53-9. PMID:9247141
