Uhlin, Ulla
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
Two nrdF genes of Mycobacterium tuberculosis code for different R2 subunits of the class Ib ribonucleotide reductase (RNR). The proteins are denoted R2F-1 and R2F-2 having 71% sequence identity. The R2F-2 subunit forms the biologically active RNR complex with the catalytic R1E-subunit. We present the structure of the reduced R2F-2 subunit to 2.2 Angstrom resolution. Comparison of the R2F-2 structure with a model of R2F-1 suggests that the important differences are located at the C-terminus. We found that within class Ib, the E-helix close to the iron diiron centre has two preferred conformations, which cannot be explained by the redox-state of the diiron centre. In the R2F-2 structure, we also could see a mobility of alphaE in between the two conformations. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Keywords
crystal structure; ribonucleotide reductase; R2; diiron carboxylate protein; tyrosyl radical; Mycobacterium tuberculosis
Published in
FEBS Letters
2004, volume: 569, number: 45660, pages: 117-122
Publisher: ELSEVIER SCIENCE BV
SLU Authors
Uppsten, Malin
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Publication identifier
- DOI: https://doi.org/10.1016/j.febslet.2004.05.059
Permanent link to this page (URI)
https://res.slu.se/id/publ/4799