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EC Number Crystallization (Commentary)
Show all pathways known for 1.2.1.105Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.105electron cryotomography, shows that the E1 and E3 subunits of the complex are flexibly tethered about 11 nm away from the E2 core
Show all pathways known for 1.2.1.105Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.105solution structure of a 51-residue synthetic peptide comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate dehydrogenase multienzyme complex
Show all pathways known for 1.2.1.105Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.105structure of the component E2 catalytic domain, to 3.0 A resolution using molecular replacement. The active site is located in the middle of a channel formed at the interface between two 3fold related subunits. Active-site residues are His375 and Thr323 and Asp379. Binding of the substrates to E2 catalytic domain is proposed to induce a change in the conformation of Asp379, allowing this residue to form a salt bridge with Arg 184. Residues Ser330, Ser333, and His348 form the succinyl-binding pocket
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