1DTS

CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION

Summary for 1DTS

Entry DOI	10.2210/pdb1dts/pdb
Descriptor	DETHIOBIOTIN SYNTHETASE (2 entities in total)
Functional Keywords	cyclo-ligase
Biological source	Escherichia coli
Cellular location	Cytoplasm: P13000
Total number of polymer chains	1
Total formula weight	23705.05
Authors	Huang, W.,Lindqvist, Y.,Schneider, G. (deposition date: 1995-03-28, release date: 1995-04-20, Last modification date: 2024-02-07)
Primary citation	Huang, W.,Lindqvist, Y.,Schneider, G.,Gibson, K.J.,Flint, D.,Lorimer, G. Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution. Structure, 2:407-414, 1994 Cited by PubMed Abstract: In Escherichia coli, the enzymes of the biotin biosynthesis pathway are encoded by the bio operon. One of these enzymes, ATP-dependent dethiobiotin synthetase, catalyzes the carboxylation of 7,8-diaminopelargonic acid leading to the formation of the ureido ring of biotin. The enzyme belongs to the class of ATP-dependent carboxylases and we present here the first crystal structure determined for this class of enzyme. PubMed: 8081756 DOI: 10.1016/S0969-2126(00)00042-3 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.65 Å)

Structure validation