Please use this identifier to cite or link to this item:
|Title:||Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23 S rRNA and is essential for normal cell growth of Escherichia coli||Authors:||Sivaraman, J.
|Issue Date:||2-Jan-2004||Citation:||Sivaraman, J., Iannuzzi, P., Cygler, M., Matte, A. (2004-01-02). Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23 S rRNA and is essential for normal cell growth of Escherichia coli. Journal of Molecular Biology 335 (1) : 87-101. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2003.10.003||Abstract:||Pseudouridine (5-β-D-ribofuranosyluracil, Ψ) is the most commonly found modified base in RNA. Conversion of uridine to Ψ is performed enzymatically in both prokaryotes and eukaryotes by pseudouridine synthases (EC 18.104.22.168). The Escherichia coli Ψ-synthase RluD modifies uridine to Ψ at positions 1911, 1915 and 1917 within 23S rRNA. RluD also possesses a second function related to proper assembly of the 50S ribosomal subunit that is independent of Ψ-synthesis. Here, we report the crystal structure of the catalytic module of RluD (residues 68-326; ΔRluD) refined at 1.8Å to a final R-factor of 21.8% (Rfree=24.3%). ΔRluD is a monomeric enzyme having an overall mixed α/β fold. The ΔRluD molecule consists of two subdomains, a catalytic subdomain and C-terminal subdomain with the RNA-binding cleft formed by loops extending from the catalytic sub-domain. The catalytic sub-domain of ΔRluD has a similar fold as in TruA, TruB and RsuA, with the location of the RNA-binding cleft, active-site and conserved, catalytic Asp residue superposing in all four structures. Superposition of the crystal structure of TruB bound to a T-stem loop with RluD reveals that similar RNA-protein interactions for the flipped-out uridine base would exist in both structures, implying that base-flipping is necessary for catalysis. This observation also implies that the specificity determinants for site-specific RNA-binding and recognition likely reside in parts of RluD beyond the active site. Crown Copyright © 2003 Published by Elsevier Ltd. All rights reserved.||Source Title:||Journal of Molecular Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/100371||ISSN:||00222836||DOI:||10.1016/j.jmb.2003.10.003|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 18, 2021
WEB OF SCIENCETM
checked on Feb 18, 2021
checked on Feb 14, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.