1NG3

Complex of ThiO (glycine oxidase) with acetyl-glycine

Summary for 1NG3

• Entry DOI: 10.2210/pdb1ng3/pdb
• Related: 1NG4
• Descriptor: Glycine oxidase, PHOSPHATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: flavoprotein, oxidase, oxidoreductase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm : O31616
• Total number of polymer chains: 2
• Total formula weight: 88999.34

Authors

Settembre, E.C.,Dorrestein, P.C.,Park, J.,Augustine, A.,Begley, T.P.,Ealick, S.E. (deposition date: 2002-12-16, release date: 2003-04-08, Last modification date: 2024-04-03)

Primary citation

Settembre, E.C.,Dorrestein, P.C.,Park, J.,Augustine, A.,Begley, T.P.,Ealick, S.E.
Structural and Mechanistic Studies on ThiO, a Glycine Oxidase Essential for Thiamin Biosynthesis in Bacillus subtilis
Biochemistry, 42:2971-2981, 2003

PubMed Abstract: The thiO gene of Bacillus subtilis encodes an FAD-dependent glycine oxidase. This enzyme is a homotetramer with a monomer molecular mass of 42 kDa. In this paper, we demonstrate that ThiO is required for the biosynthesis of the thiazole moiety of thiamin pyrophosphate and describe the structure of the enzyme with N-acetylglycine bound at the active site. The closest structural relatives of ThiO are sarcosine oxidase and d-amino acid oxidase. The ThiO structure, as well as the observation that N-cyclopropylglycine is a good substrate, supports a hydride transfer mechanism for the enzyme. A mechanistic proposal for the role of ThiO in thiazole biosynthesis is also described.

PubMed: 12627963
DOI: 10.1021/bi026916v

Experimental method

X-RAY DIFFRACTION (2.6 Å)