1q5x
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(New page: 200px<br /><applet load="1q5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q5x, resolution 2.0Å" /> '''Structure of OF RRAA ...)
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Revision as of 22:17, 20 November 2007
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Structure of OF RRAA (MENG), a protein inhibitor of RNA processing
Overview
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.
About this Structure
1Q5X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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