2GML

Crystal Structure of Catalytic Domain of E.coli RluF

Summary for 2GML

• Entry DOI: 10.2210/pdb2gml/pdb
• Descriptor: Ribosomal large subunit pseudouridine synthase F (2 entities in total)
• Functional Keywords: pseudouridine synthase, rluf, ribosome, rna modifying enzyme, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 53635.01

Authors

Sunita, S.,Zhenxing, H.,Swaathi, J.,Cygler, M.,Matte, A.,Sivaraman, J. (deposition date: 2006-04-06, release date: 2006-07-18, Last modification date: 2011-07-13)

Primary citation

Sunita, S.,Zhenxing, H.,Swaathi, J.,Cygler, M.,Matte, A.,Sivaraman, J.
Domain Organization and Crystal Structure of the Catalytic Domain of E.coli RluF, a Pseudouridine Synthase that Acts on 23S rRNA
J.Mol.Biol., 359:998-1009, 2006

PubMed Abstract: 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.

PubMed: 16712869
DOI: 10.1016/j.jmb.2006.04.019

Experimental method

X-RAY DIFFRACTION (2.6 Å)