Literature summary for 1.2.1.105 extracted from

Knapp, J.E.; Mitchell, D.T.; Yazdi, M.A.; Ernst, S.R.; Reed, L.J.; Hackert, M.L.
Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex (1998), J. Mol. Biol., 280, 655-668 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure 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	Escherichia coli

Crystallization (Comment)

Organism

structure 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

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFG6	i.e. SucB, dihydrolipoyllysine-residue succinyltransferase component E2, cf. EC 2.3.1.61	-

Synonyms

Synonyms	Comment	Organism
SucB	-	Escherichia coli

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Release 2023.1 (January 2023)