2gml
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(New page: 200px<br /><applet load="2gml" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gml, resolution 2.6Å" /> '''Crystal Structure of ...)
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Revision as of 09:09, 21 November 2007
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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
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