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| - | [[Image:2frx.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2frx| PDB=2frx | SCENE= }} | | {{STRUCTURE_2frx| PDB=2frx | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16793063}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16793063 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16793063}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nordlund, P.]] | | [[Category: Nordlund, P.]] |
| | [[Category: Rossmann-type s-adenosylmethionine-dependent methyltransferase domain]] | | [[Category: Rossmann-type s-adenosylmethionine-dependent methyltransferase domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:14:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:19:24 2008'' |
Revision as of 01:19, 28 July 2008
Template:STRUCTURE 2frx
Crystal structure of YebU, a m5C RNA methyltransferase from E.coli
Template:ABSTRACT PUBMED 16793063
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 Mon Jul 28 04:19:24 2008
