1DBS
MECHANISTIC IMPLICATIONS AND FAMILY RELATIONSHIPS FROM THE STRUCTURE OF DETHIOBIOTIN SYNTHETASE
Summary for 1DBS
Entry DOI | 10.2210/pdb1dbs/pdb |
Descriptor | DETHIOBIOTIN SYNTHETASE, SULFATE ION (3 entities in total) |
Functional Keywords | biotin biosynthesis |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P13000 |
Total number of polymer chains | 1 |
Total formula weight | 24316.48 |
Authors | Sawyer, L.,Alexeev, D. (deposition date: 1994-11-29, release date: 1995-04-20, Last modification date: 2024-02-07) |
Primary citation | Alexeev, D.,Baxter, R.L.,Sawyer, L. Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Structure, 2:1061-1072, 1994 Cited by PubMed Abstract: Biotin is the vitamin essential for many biological carboxylation reactions, such as the conversion of acetyl-coenzyme A (CoA) to malonyl-CoA in fatty acid biosynthesis. Dethiobiotin synthetase (DTBS) facilitates the penultimate, ureido ring closure in biotin synthesis, which is a non-biotin-dependent carboxylation. DTBS displays no sequence similarity to any other protein in the database. Structural studies provide a molecular insight into the reaction mechanism of DTBS. PubMed: 7881906DOI: 10.1016/S0969-2126(94)00109-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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