1J3L

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

Summary for 1J3L

• Entry DOI: 10.2210/pdb1j3l/pdb
• Descriptor: Demethylmenaquinone Methyltransferase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: vitamine k2, structural genomics, riken structural genomics/proteomics initiative, rsgi, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 6
• Total formula weight: 104836.31

Authors

Rehse, P.H.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-02-04, release date: 2004-02-17, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)