NDLI: NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.

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NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.

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NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tamu Dufe, Veronica Hbeddou, Abderahim Van Laer, Koen Collet, Jean-francois Dziewulska, Aleksandra M. Versées, Wim Mateos, Luis M. Messens, Joris Wahni, Khadija Fislage, Marcus
Description	Author Affiliation: Van Laer K ( Department of Structural Biology, Vlaams Instituut voor Biotechnologie, 1050 Brussels, Belgium.)
Abstract	NrdH-redoxins are small reductases with a high amino acid sequence similarity with glutaredoxins and mycoredoxins but with a thioredoxin-like activity. They function as the electron donor for class Ib ribonucleotide reductases, which convert ribonucleotides into deoxyribonucleotides. We solved the x-ray structure of oxidized NrdH-redoxin from Corynebacterium glutamicum (Cg) at 1.5 â « resolution. Based on this monomeric structure, we built a homology model of NrdH-redoxin from Mycobacterium tuberculosis (Mt). Both NrdH-redoxins have a typical thioredoxin fold with the active site CXXC motif located at the N terminus of the first -helix. With size exclusion chromatography and small angle x-ray scattering, we show that Mt_NrdH-redoxin is a monomer in solution that has the tendency to form a non-swapped dimer at high protein concentration. Further, Cg_NrdH-redoxin and Mt_NrdH-redoxin catalytically reduce a disulfide with a specificity constant 1.9 × 10(6) and 5.6 × 10(6) M(-1) min(-1), respectively. They use a thiol-disulfide exchange mechanism with an N-terminal cysteine pKa lower than 6.5 for nucleophilic attack, whereas the pKa of the C-terminal cysteine is ~10. They exclusively receive electrons from thioredoxin reductase (TrxR) and not from mycothiol, the low molecular weight thiol of actinomycetes. This specificity is shown in the structural model of the complex between NrdH-redoxin and TrxR, where the two surface-exposed phenylalanines of TrxR perfectly fit into the conserved hydrophobic pocket of the NrdH-redoxin. Moreover, nrdh gene deletion and disruption experiments seem to indicate that NrdH-redoxin is essential in C. glutamicum.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	11
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-03-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Corynebacterium Glutamicum Metabolism Escherichia Coli Proteins Mycobacterium Tuberculosis Thioredoxins Amino Acid Sequence Antitubercular Agents Pharmacology Catalytic Domain Cloning, Molecular Crystallography, X-Ray Cysteine Chemistry Dimerization Electrons Glycopeptides Hydrogen-Ion Concentration Inositol Kinetics Molecular Conformation Molecular Sequence Data Oxidation-Reduction Protein Binding Protein Structure, Tertiary Ribonucleotides Scattering, Radiation Sequence Homology, Amino Acid Surface Properties Thioredoxin-Disulfide Reductase X-Rays Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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