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Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii

¹ Department of Chemistry, University of California at Berkeley, Berkeley, California 94720-1460, USA
² Physical Bioscience Division, Calvin Laboratory, Lawrence Berkeley National Laboratory, Berkeley, California 94720–5230, USA

Reprint requests to: David E. Wemmer, Department of Chemistry, MC-1460, University of California at Berkeley, Berkeley, California 94720–1460, USA; e-mail: DEWemmer{at}lbl.gov; fax: 510-486-6059.

The solution structure of the protein disulfide oxidoreductase Mj0307 in the reduced form has been solved by nuclear magnetic resonance. The secondary and tertiary structure of this protein from the archaebacterium Methanococcus jannaschii is similar to the structures that have been solved for the glutaredoxin proteins from Escherichia coli, although Mj0307 also shows features that are characteristic of thioredoxin proteins. Some aspects of Mj0307's unique behavior can be explained by comparing structure-based sequence alignments with mesophilic bacterial and eukaryotic glutaredoxin and thioredoxin proteins. It is proposed that Mj0307, and similar archaebacterial proteins, may be most closely related to the mesophilic bacterial NrdH proteins. Together these proteins may form a unique subgroup within the family of protein disulfide oxidoreductases.

Keywords: Protein oxidoreductase; NMR structure; thioredoxin homolog; thermophile

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