1dam

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spinqualitylabelsall models 1dam, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC PHOSPHATE AND MAGNESIUM

Overview

The crystal structures of two complexes of dethiobiotin synthetase, enzyme-diaminopelargonic acid-MgADP-AlF3 and enzyme-dethiobiotin-MgADP-Pi, respectively, have been determined to 1.8 A resolution. In dethiobiotin, synthetase, AlF3 together with carbamylated diaminopelargonic acid mimics, the phosphorylated reaction intermediate rather than the transition state, complex for phosphoryl transfer. Observed differences in the binding of, substrate, diaminopelargonic acid, and the product, dethiobiotin, suggest, considerable displacements of substrate atoms during the ring closure step, of the catalytic reaction. In both complexes, two metal ions are observed, at the active site, providing evidence for a two-metal mechanism for this, enzyme.

About this Structure

1DAM is a Single protein structure of sequence from Escherichia coli with MG, PO4, ADP and DTB as ligands. Active as Dethiobiotin synthase, with EC number 6.3.3.3 Full crystallographic information is available from OCA.

Reference

Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis., Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y, Protein Sci. 1998 Dec;7(12):2560-6. PMID:9865950

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