Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jmb.2006.04.019
Title: Domain Organization and Crystal Structure of the Catalytic Domain of E. coli RluF, a Pseudouridine Synthase that Acts on 23S rRNA
Authors: Sunita, S.
Zhenxing, H.
Swaathi, J.
Cygler, M.
Matte, A.
Sivaraman, J. 
Keywords: crystal structure
pseudouridine synthase
ribosome
RluF
RNA modifying enzyme
Issue Date: 16-Jun-2006
Citation: Sunita, S., Zhenxing, H., Swaathi, J., Cygler, M., Matte, A., Sivaraman, J. (2006-06-16). Domain Organization and Crystal Structure of the Catalytic Domain of E. coli RluF, a Pseudouridine Synthase that Acts on 23S rRNA. Journal of Molecular Biology 359 (4) : 998-1009. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2006.04.019
Abstract: Pseudouridine synthases catalyze the isomerization of uridine to pseudouridine (Ψ) in rRNA and tRNA. The pseudouridine synthase RluF from Escherichia coli (E.C. 4.2.1.70) modifies U2604 in 23S rRNA, and belongs to a large family of pseudouridine synthases present in all kingdoms of life. Here we report the domain architecture and crystal structure of the catalytic domain of E. coli RluF at 2.6 Å resolution. Limited proteolysis, mass spectrometry and N-terminal sequencing indicate that RluF has a distinct domain architecture, with the catalytic domain flanked at the N and C termini by additional domains connected to it by flexible linkers. The structure of the catalytic domain of RluF is similar to those of RsuA and TruB. RluF is a member of the RsuA sequence family of Ψ-synthases, along with RluB and RluE. Structural comparison of RluF with its closest structural homologues, RsuA and TruB, suggests possible functional roles for the N-terminal and C-terminal domains of RluF. © 2006 Elsevier Ltd. All rights reserved.
Source Title: Journal of Molecular Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/100499
ISSN: 00222836
DOI: 10.1016/j.jmb.2006.04.019
Appears in Collections:Staff Publications

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

SCOPUSTM   
Citations

11
checked on Sep 29, 2022

WEB OF SCIENCETM
Citations

10
checked on Sep 29, 2022

Page view(s)

138
checked on Sep 22, 2022

Google ScholarTM

Check

Altmetric


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