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1q5x
From Proteopedia
Revision as of 16:32, 29 September 2014 by OCA (Talk | contribs)
1q5x is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing in vivo and in vitro. Here, we report the 2.0A X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12A in diameter. Based on earlier sequence analysis, RraA had been identified as a putative S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the E.coli RraA exhibits an ancient relationship to a family of aldolases.
The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing.,Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD J Mol Biol. 2003 Oct 3;332(5):1015-24. PMID:14499605[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD. The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing. J Mol Biol. 2003 Oct 3;332(5):1015-24. PMID:14499605
