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|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. |
|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 220.127.116.11). 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|
|Appears in Collections:||Staff Publications|
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