1q5x

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|ACTIVITY=
|ACTIVITY=
|GENE= MENG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= MENG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5x OCA], [http://www.ebi.ac.uk/pdbsum/1q5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q5x RCSB]</span>
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[[Category: parallel beta sheet]]
[[Category: parallel beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:13 2008''

Revision as of 20:09, 30 March 2008


PDB ID 1q5x

Drag the structure with the mouse to rotate
, resolution 2.0Å
Gene: MENG (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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