1DAM

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

Summary for 1DAM

• Entry DOI: 10.2210/pdb1dam/pdb
• Descriptor: PROTEIN (DETHIOBIOTIN SYNTHETASE), MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: ligase, biotin biosynthesis, magnesium, atp-binding, phosphoryl transfer
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P13000
• Total number of polymer chains: 1
• Total formula weight: 24813.33

Authors

Kaeck, H.,Sandmark, J.,Gibson, K.J.,Schneider, G.,Lindqvist, Y. (deposition date: 1998-08-31, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

Kack, H.,Sandmark, J.,Gibson, K.J.,Schneider, G.,Lindqvist, Y.
Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis.
Protein Sci., 7:2560-2566, 1998

PubMed Abstract: 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.

PubMed: 9865950

Experimental method

X-RAY DIFFRACTION (1.8 Å)