1q5x
From Proteopedia
(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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1q5x.jpg|left|200px]]<br /><applet load="1q5x" size=" | + | [[Image:1q5x.jpg|left|200px]]<br /><applet load="1q5x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q5x, resolution 2.0Å" /> | caption="1q5x, resolution 2.0Å" /> | ||
'''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing'''<br /> | '''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Escherichia coli protein regulator of RNase E activity A (RraA) has | + | 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== | ==About this Structure== | ||
| - | 1Q5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1Q5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5X OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Gao, J.]] | [[Category: Gao, J.]] | ||
[[Category: Georgiou, G.]] | [[Category: Georgiou, G.]] | ||
| - | [[Category: Monzingo, A | + | [[Category: Monzingo, A F.]] |
[[Category: Qiu, J.]] | [[Category: Qiu, J.]] | ||
| - | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: 3-layer sandwich]] | [[Category: 3-layer sandwich]] | ||
[[Category: alpha-beta structure]] | [[Category: alpha-beta structure]] | ||
| Line 23: | Line 23: | ||
[[Category: parallel beta sheet]] | [[Category: parallel beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:16 2008'' |
Revision as of 12:36, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 14:36:16 2008
