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PDBsum entry 2g0c
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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S.Wang,
Y.Hu,
M.T.Overgaard,
F.V.Karginov,
O.C.Uhlenbeck,
D.B.Mckay.
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Ref.
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Rna, 2006,
12,
959-967.
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PubMed id
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Abstract
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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.
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