Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

Peter H. Rehse, Chizu Kuroishi, Tahir H. Tahirov

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Abstract

The menG gene product, thought to catalyze the final methylation in vitamin K2 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 Å 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.

Original languageEnglish (US)
Pages (from-to)1997-2002
Number of pages6
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number11
DOIs
Publication statusPublished - Nov 1 2004

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ASJC Scopus subject areas

  • Structural Biology

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