Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.
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.
Cave
J W
JW
Department of Chemistry, University of California at Berkeley, Berkeley, California 94720-1460, USA.
Cho
H S
HS
Batchelder
A M
AM
Yokota
H
H
Kim
R
R
Wemmer
D E
DE
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004220:Disulfides; D004926:Escherichia coli / Q000737:chemistry; D054477:Glutaredoxins; D009682:Magnetic Resonance Spectroscopy; D017017:Methanococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D010088:Oxidoreductases; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D013879:Thioredoxins / Q000737:chemistry
D004220:Disulfides; D054477:Glutaredoxins; D011506:Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D009247:NADH, NADPH Oxidoreductases; C431348:protein disulfide oxidoreductase, Methanococcus jannaschii