3tg8

Mutant ribosomal protein L1 lacking ala158 from thermus thermophilusMutant ribosomal protein L1 lacking ala158 from thermus thermophilus

Structural highlights 3tg8 is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 1ad2 Gene: rplA, rpl1 ("Flavobacterium thermophilum" Yoshida and Oshima 1971) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] Publication Abstract from PubMed Ribosomal protein L1 consists of two domains connected by two oppositely directed fragments of the polypeptide chain in a hinge-resembling fashion. The domain arrangement determines the overall shape of the protein, corresponding to an open or a closed conformation. Ribosomal L1 proteins from archaea demonstrate the open conformation in both isolated and RNA-bound forms. RNA-free ribosomal L1 proteins from bacteria display the closed conformation, whereas in complex with RNA these proteins exist in an open conformation similar to their archaeal counterparts. Analysis of all available L1 amino-acid sequences shows that in comparison to the archaeal proteins, the bacterial proteins possess an extra residue in one of the two interdomain fragments which could be responsible for their closed conformation. To verify this suggestion, a Thermus thermophilus L1 mutant lacking one residue in the fragment corresponding to the hinge was obtained and its crystal structure was solved. It was found that this mutation transformed the closed conformation of the bacterial L1 protein into an open conformation similar to that of the archaeal L1 proteins. Structural analysis of interdomain mobility in ribosomal L1 proteins.,Tishchenko S, Nikonova E, Kostareva O, Gabdulkhakov A, Piendl W, Nevskaya N, Garber M, Nikonov S Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1023-7. Epub 2011 Nov 5. PMID:22120739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L1

spinqualitylabelsall models 3tg8, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image