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Literature summary for 1.1.1.305 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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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

Organism

Organism UniProt Comment Textmining
Escherichia coli P77398
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Synonyms

Synonyms Comment Organism
ArnA
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Escherichia coli