Literature summary for 2.1.2.13 extracted from

Fischer, U.; Hertlein, S.; Grimm, C.
The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity (2015), Acta Crystallogr. Sect. D, 71, 687-696.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of apo-ArnA and comparison with its ATP- and UDP-glucuronic acid-bound counterparts. In the crystal structure, a binding pocket at the centre of each ArnA trimer in its apo state pocket is occupied by a dithiothreitol molecule. Formation of the pocket is linked to a cascade of structural rearrangements that emerge from the NAD+-binding site. A small effector molecule is postulated that binds to the central pocket and modulates the catalytic properties of ArnA	Escherichia coli

Crystallization (Comment)

Organism

structure of apo-ArnA and comparison with its ATP- and UDP-glucuronic acid-bound counterparts. In the crystal structure, a binding pocket at the centre of each ArnA trimer in its apo state pocket is occupied by a dithiothreitol molecule. Formation of the pocket is linked to a cascade of structural rearrangements that emerge from the NAD+-binding site. A small effector molecule is postulated that binds to the central pocket and modulates the catalytic properties of ArnA

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P77398	-	-

Synonyms

Synonyms	Comment	Organism
ArnA	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2026.1 (March 2026)