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Structure of the RNA-processing inhibitor RraA from Thermus thermophilisStructure of the RNA-processing inhibitor RraA from Thermus thermophilis
Structural highlights
FunctionRRAAH_THET8 Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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