1q5x
From Proteopedia
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| - | [[Image:1q5x.jpg|left|200px]] | + | [[Image:1q5x.jpg|left|200px]] |
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| - | '''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing''' | + | {{Structure |
| + | |PDB= 1q5x |SIZE=350|CAPTION= <scene name='initialview01'>1q5x</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= MENG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q5X is a [ | + | 1Q5X is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14499605 14499605] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: parallel beta sheet]] | [[Category: parallel beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:24 2008'' |
Revision as of 11:33, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Gene: | MENG (Escherichia coli) | ||||||
| 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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