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Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L242M)Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L242M)
Structural highlights
FunctionDPHB_PYRHO S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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