1ng3

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(New page: 200px<br /><applet load="1ng3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ng3, resolution 2.60&Aring;" /> '''Complex of ThiO (gly...)
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Revision as of 20:06, 20 November 2007

Image:1ng3.jpg

1ng3, resolution 2.60Å

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Complex of ThiO (glycine oxidase) with acetyl-glycine

Overview

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.

About this Structure

1NG3 is a Single protein structure of sequence from Bacillus subtilis with PO4, FAD and AAC as ligands. Full crystallographic information is available from OCA.

Reference

Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis., Settembre EC, Dorrestein PC, Park JH, Augustine AM, Begley TP, Ealick SE, Biochemistry. 2003 Mar 18;42(10):2971-81. PMID:12627963

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