2frx

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[[Image:2frx.gif|left|200px]]
[[Image:2frx.gif|left|200px]]
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{{Structure
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|GENE= YebU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2frx| PDB=2frx | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2frx OCA], [http://www.ebi.ac.uk/pdbsum/2frx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2frx RCSB]</span>
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'''Crystal structure of YebU, a m5C RNA methyltransferase from E.coli'''
'''Crystal structure of YebU, a m5C RNA methyltransferase from E.coli'''
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[[Category: Johnson, K A.]]
[[Category: Johnson, K A.]]
[[Category: Nordlund, P.]]
[[Category: Nordlund, P.]]
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[[Category: c-terminal pua (pseudouridine synthases and archaeosine-specific transglycosylases) domain]]
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[[Category: Rossmann-type s-adenosylmethionine-dependent methyltransferase domain]]
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[[Category: rossmann-type s-adenosylmethionine-dependent methyltransferase domain]]
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Revision as of 01:14, 4 May 2008

Template:STRUCTURE 2frx

Crystal structure of YebU, a m5C RNA methyltransferase from E.coli


Overview

Nucleotide methylations are the most common type of rRNA modification in bacteria, and are introduced post-transcriptionally by a wide variety of site-specific enzymes. Three 5-methylcytidine (m(5)C) bases are found in the rRNAs of Escherichia coli and one of these, at nucleotide 1407 in 16 S rRNA, is the modification product of the methyltransferase (MTase) YebU (also called RsmF). YebU requires S-adenosyl-l-methionine (SAM) and methylates C1407 within assembled 30 S subunits, but not in naked 16 S rRNA or within tight-couple 70 S ribosomes. Here, we describe the three-dimensional structure of YebU determined by X-ray crystallography, and we present a molecular model for how YebU specifically recognizes, binds and methylates its ribosomal substrate. The YebU protein has an N-terminal SAM-binding catalytic domain with structural similarity to the equivalent domains in several other m(5)C RNA MTases including RsmB and PH1374. The C-terminal one-third of YebU contains a domain similar to that in pseudouridine synthases and archaeosine-specific transglycosylases (PUA-domain), which was not predicted by sequence alignments. Furthermore, YebU is predicted to contain extended regions of positive electrostatic potential that differ from other RNA-MTase structures, suggesting that YebU interacts with its RNA target in a different manner. Docking of YebU onto the 30 S subunit indicates that the PUA and MTase domains make several contacts with 16 S rRNA as well as with the ribosomal protein S12. The ribosomal protein interactions would explain why the assembled 30 S subunit, and not naked 16 S rRNA, is the preferred substrate for YebU.

About this Structure

2FRX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals a C-terminal RNA-recruiting PUA domain., Hallberg BM, Ericsson UB, Johnson KA, Andersen NM, Douthwaite S, Nordlund P, Beuscher AE 4th, Erlandsen H, J Mol Biol. 2006 Jul 21;360(4):774-87. Epub 2006 Jun 6. PMID:16793063 Page seeded by OCA on Sun May 4 04:14:28 2008

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