1J3L

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

1J3L の概要

• エントリーDOI: 10.2210/pdb1j3l/pdb
• 分子名称: Demethylmenaquinone Methyltransferase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: vitamine k2, structural genomics, riken structural genomics/proteomics initiative, rsgi, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 104836.31

構造登録者

Rehse, P.H.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-02-04, 公開日: 2004-02-17, 最終更新日: 2024-10-30)

主引用文献

Rehse, P.H.,Kuroishi, C.,Tahirov, T.H.
Structure of the RNA-processing inhibitor RraA from Thermus thermophilis.
Acta Crystallogr.,Sect.D, 60:1997-2002, 2004

PubMed Abstract: The menG gene product, thought to catalyze the final methylation in vitamin K(2) synthesis, has recently been shown to inhibit RNase E in Eschericha coli. The structure of the protein, since renamed RraA, has been solved to 2.3 A using the multiple-wavelength anomalous diffraction method and selenomethionine-substituted protein from Thermus thermophilus. The six molecules in the asymmetric unit are arranged as two similar trimers which have a degree of interaction, suggesting biological significance. The fold does not support the postulated methylation function. Genomic analysis, specifically a lack of an RNase E homologue in cases where homologues to RraA exist, indicates that the function is still obscure.

PubMed: 15502308
DOI: 10.1107/S0907444904021146

実験手法

X-RAY DIFFRACTION (2.3 Å)