2gml

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'''Crystal Structure of Catalytic Domain of E.coli RluF'''
'''Crystal Structure of Catalytic Domain of E.coli RluF'''
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[[Category: Swaathi, J.]]
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[[Category: Crystal structure]]
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[[Category: pseudouridine synthase]]
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[[Category: Pseudouridine synthase]]
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[[Category: ribosome]]
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[[Category: rluf]]
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[[Category: Rluf]]
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[[Category: rna modifying enzyme]]
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Revision as of 02:16, 4 May 2008

Template:STRUCTURE 2gml

Crystal Structure of Catalytic Domain of E.coli RluF


Overview

Pseudouridine synthases catalyze the isomerization of uridine to pseudouridine (Psi) 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 2.6A 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 Psi-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.

About this Structure

2GML is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA., Sunita S, Zhenxing H, Swaathi J, Cygler M, Matte A, Sivaraman J, J Mol Biol. 2006 Jun 16;359(4):998-1009. Epub 2006 Apr 25. PMID:16712869 Page seeded by OCA on Sun May 4 05:16:36 2008

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