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1DAK

DETHIOBIOTIN SYNTHETASE FROM ESCHERICHIA COLI, COMPLEX REACTION INTERMEDIATE ADP AND MIXED ANHYDRIDE

Summary for 1DAK
Entry DOI10.2210/pdb1dak/pdb
DescriptorDETHIOBIOTIN SYNTHETASE, PHOSPHATE ION, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsphoshporyl transfer, biotin biosynthesis, ligase, kinetic crystallography
Biological sourceEscherichia coli
Cellular locationCytoplasm: P13000
Total number of polymer chains1
Total formula weight24911.33
Authors
Kaeck, H.,Gibson, K.J.,Lindqvist, Y.,Schneider, G. (deposition date: 1998-03-31, release date: 1999-04-06, Last modification date: 2024-05-22)
Primary citationKack, H.,Gibson, K.J.,Lindqvist, Y.,Schneider, G.
Snapshot of a phosphorylated substrate intermediate by kinetic crystallography.
Proc.Natl.Acad.Sci.USA, 95:5495-5500, 1998
Cited by
PubMed Abstract: The ATP-dependent enzyme dethiobiotin synthetase from Escherichia coli catalyses the formation of dethiobiotin from CO2 and 7, 8-diaminopelargonic acid. The reaction is initiated by the formation of a carbamate and proceeds through a phosphorylated intermediate, a mixed carbamic phosphoric anhydride. Here, we report the crystal structures at 1.9- and 1.6-A resolution, respectively, of the enzyme-MgATP-diaminopelargonic acid and enzyme-MgADP-carbamic-phosphoric acid anhydride complexes, observed by using kinetic crystallography. Reaction initiation by addition of either NaHCO3 or diaminopelargonic acid to crystals already containing cosubstrates resulted in the accumulation of the phosphorylated intermediate at the active site. The phosphoryl transfer step shows inversion of the configuration at the phosphorus atom, consistent with an in-line attack by the carbamate oxygen onto the phosphorus atom of ATP. A key feature in the structure of the complex of the enzyme with the reaction intermediate is two magnesium ions, bridging the phosphates at the cleavage site. These magnesium ions compensate the negative charges at both phosphate groups after phosphoryl transfer and contribute to the stabilization of the reaction intermediate.
PubMed: 9576910
DOI: 10.1073/pnas.95.10.5495
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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