Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jmb.2008.08.062
Title: Crystal Structure of the Escherichia coli 23S rRNA:m5C Methyltransferase RlmI (YccW) Reveals Evolutionary Links between RNA Modification Enzymes
Authors: Sunita, S.
Tkaczuk, K.L.
Purta, E.
Kasprzak, J.M.
Douthwaite, S.
Bujnicki, J.M.
Sivaraman, J. 
Keywords: crystal structure
methyltransferase
RlmI
rRNA modification
YccW
Issue Date: 14-Nov-2008
Source: Sunita, S., Tkaczuk, K.L., Purta, E., Kasprzak, J.M., Douthwaite, S., Bujnicki, J.M., Sivaraman, J. (2008-11-14). Crystal Structure of the Escherichia coli 23S rRNA:m5C Methyltransferase RlmI (YccW) Reveals Evolutionary Links between RNA Modification Enzymes. Journal of Molecular Biology 383 (3) : 652-666. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2008.08.062
Abstract: Methylation is the most common RNA modification in the three domains of life. Transfer of the methyl group from S-adenosyl-l-methionine (AdoMet) to specific atoms of RNA nucleotides is catalyzed by methyltransferase (MTase) enzymes. The rRNA MTase RlmI (rRNA large subunit methyltransferase gene I; previously known as YccW) specifically modifies Escherichia coli 23S rRNA at nucleotide C1962 to form 5-methylcytosine. Here, we report the crystal structure of RlmI refined at 2 Å to a final R-factor of 0.194 (Rfree = 0.242). The RlmI molecule comprises three domains: the N-terminal PUA domain; the central domain, which resembles a domain previously found in RNA:5-methyluridine MTases; and the C-terminal catalytic domain, which contains the AdoMet-binding site. The central and C-terminal domains are linked by a β-hairpin structure that has previously been observed in several MTases acting on nucleic acids or proteins. Based on bioinformatics analyses, we propose a model for the RlmI-AdoMet-RNA complex. Comparative structural analyses of RlmI and its homologs provide insight into the potential function of several structures that have been solved by structural genomics groups and furthermore indicate that the evolutionary paths of RNA and DNA 5-methyluridine and 5-methylcytosine MTases have been closely intertwined. © 2008 Elsevier Ltd. All rights reserved.
Source Title: Journal of Molecular Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/100367
ISSN: 00222836
DOI: 10.1016/j.jmb.2008.08.062
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

25
checked on Feb 20, 2018

WEB OF SCIENCETM
Citations

23
checked on Nov 21, 2017

Page view(s)

31
checked on Feb 16, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.