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2gjc

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2gjc, resolution 1.82Å

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Crystal Structure of Thiazole Synthase in Saccharomyces cerevisiae at 1.82 A resolution

Overview

The structure of thiazole synthase (Thi4) from Saccharomyces cerevisiae, was determined to 1.8 A resolution. Thi4 exists as an octamer with two, monomers in the asymmetric unit. The structure reveals the presence of a, tightly bound adenosine, diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid at the active, site. The isolation of this reaction product identifies NAD as the most, likely precursor and provides the first mechanistic insights into the, biosynthesis of the thiamin thiazole in eukaryotes. Additionally, the Thi4, structure reveals the first protein structure with a GR(2) domain that, binds NAD instead of FAD, raising interesting questions about how this, protein evolved from a flavoenzyme to a NAD binding enzyme.

About this Structure

2GJC is a Single protein structure of sequence from Saccharomyces cerevisiae with AHZ as ligand. Full crystallographic information is available from OCA.

Reference

Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae., Jurgenson CT, Chatterjee A, Begley TP, Ealick SE, Biochemistry. 2006 Sep 19;45(37):11061-70. PMID:16964967

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