This family includes prokaryotic L1 and eukaryotic L10.
Ribosomal protein L1 is the largest protein from the large ribosomal subunit. The L1 protein contains two domains: 2-layer alpha/beta domain and a 3-layer alpha/beta domain (interrupts the first domain). The two domains cycle between open and closed conformations via a hinge motion. In Escherichia coli, L1 is known to bind to the 23S rRNA. The RNA-binding site of L1 is highly conserved, with both mRNA and rRNA binding the same binding site. Like several other large ribosomal subunit proteins, L1 displays RNA chaperone activity [PUBMED:17517772,PUBMED:15659579,PUBMED:16330048,PUBMED:12037305, PUBMED:10801481,PUBMED:12514741]. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [PUBMED:8635468, PUBMED:8607874], groups:
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