2g0c
From Proteopedia
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Structure of the RNA binding domain (residues 404-479) of the Bacillus subtilis YxiN protein
Overview
The YxiN protein of Bacillus subtilis is a member of the DbpA subfamily of, prokaryotic DEAD-box RNA helicases. Like DbpA, it binds with high affinity, and specificity to segments of 23S ribosomal RNA as short as 32, nucleotides (nt) that include hairpin 92. Several experiments have shown, that the 76-residue carboxy-terminal domain of YxiN is responsible for the, high-affinity RNA binding. The domain has been crystallized and its, structure has been solved to 1.7 Angstroms resolution. The structure, reveals an RNA recognition motif (RRM) fold that is found in many, eukaryotic RNA binding proteins; the RRM fold was not apparent from the, amino acid sequence. The domain has two solvent exposed aromatic residues, at sites that correspond to the aromatic residues of the ribonucleoprotein, (RNP) motifs RNP1 and RNP2 that are essential for RNA binding in many, RRMs. However, mutagenesis of these residues (Tyr404 and Tyr447) to, alanine has little effect on RNA affinity, suggesting that the YxiN domain, binds target RNAs in a manner that differs from the binding mode commonly, found in many eukaryotic RRMs.
About this Structure
2G0C is a Single protein structure of sequence from Bacillus subtilis with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold., Wang S, Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC, McKay DB, RNA. 2006 Jun;12(6):959-67. Epub 2006 Apr 12. PMID:16611943
Page seeded by OCA on Wed Nov 21 10:52:38 2007
