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1j3l

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Template:STRUCTURE 1j3l

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis


Overview

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.

About this Structure

1J3L is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis., Rehse PH, Kuroishi C, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1997-2002. Epub, 2004 Oct 20. PMID:15502308 Page seeded by OCA on Fri May 2 20:45:54 2008

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