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2gjc
From Proteopedia
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| , resolution 1.82Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | THI4 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 03:17:30 2008
