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Literature summary for 6.3.2.1 extracted from

  • Chakrabarti, K.S.; Thakur, K.G.; Gopal, B.; Sarma, S.P.
    X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate (2010), FEBS J., 277, 697-712.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
tertiary structure of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase, to a resolution of 1.7 A, shows a second molecule of pantoate bound in the ATP-binding pocket. Pantoate binding to the ATP-binding site induces large changes in structure, mainly for backbone and side chain atoms of residues in the ATP binding HXGH(34-37) motif. ATP stoichiometrically displaces pantoate from the ATP-binding site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P31663
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