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NMR STRUCTURES OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXINNMR STRUCTURES OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN
Structural highlights
FunctionGLRX_BPT4 Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References |
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