2G0C

Structure of the RNA binding domain (residues 404-479) of the Bacillus subtilis YxiN protein

2G0C の概要

• エントリーDOI: 10.2210/pdb2g0c/pdb
• 分子名称: ATP-dependent RNA helicase dbpA, SULFATE ION (3 entities in total)
• 機能のキーワード: rna recognition motif, hydrolase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P42305
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8484.01

構造登録者

McKay, D.B. (登録日: 2006-02-11, 公開日: 2006-04-18, 最終更新日: 2024-04-03)

主引用文献

Wang, S.,Hu, Y.,Overgaard, M.T.,Karginov, F.V.,Uhlenbeck, O.C.,McKay, D.B.
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.
RNA, 12:959-967, 2006

PubMed Abstract: 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.

PubMed: 16611943
DOI: 10.1261/rna.5906

実験手法

X-RAY DIFFRACTION (1.7 Å)