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1DBS

MECHANISTIC IMPLICATIONS AND FAMILY RELATIONSHIPS FROM THE STRUCTURE OF DETHIOBIOTIN SYNTHETASE

Summary for 1DBS
Entry DOI10.2210/pdb1dbs/pdb
DescriptorDETHIOBIOTIN SYNTHETASE, SULFATE ION (3 entities in total)
Functional Keywordsbiotin biosynthesis
Biological sourceEscherichia coli
Cellular locationCytoplasm: P13000
Total number of polymer chains1
Total formula weight24316.48
Authors
Sawyer, L.,Alexeev, D. (deposition date: 1994-11-29, release date: 1995-04-20, Last modification date: 2024-02-07)
Primary citationAlexeev, 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: 7881906
DOI: 10.1016/S0969-2126(94)00109-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

226707

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