3FPZ

Saccharomyces cerevisiae THI4p is a suicide thiamin thiazole synthase

Replaces:  2GJC

Summary for 3FPZ

• Entry DOI: 10.2210/pdb3fpz/pdb
• Related: 1RP0 2GJC
• Descriptor: Thiazole biosynthetic enzyme, ADENOSINE DIPHOSPHATE 5-(BETA-ETHYL)-4-METHYL-THIAZOLE-2-CARBOXYLIC ACID, SULFATE ION, ... (4 entities in total)
• Functional Keywords: thiazole biosynthetic enzyme in yeast, fad, mitochondrion, nad, thiamine biosynthesis, transit peptide, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: P32318
• Total number of polymer chains: 2
• Total formula weight: 71466.55

Authors

Bale, S.,Chatterjee, A.,Dorrestein, P.C.,Begley, T.P.,Ealick, S.E. (deposition date: 2009-01-06, release date: 2010-01-19, Last modification date: 2023-09-06)

Primary citation

Chatterjee, A.,Abeydeera, N.D.,Bale, S.,Pai, P.J.,Dorrestein, P.C.,Russell, D.H.,Ealick, S.E.,Begley, T.P.
Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase.
Nature, 478:542-546, 2011

PubMed Abstract: Thiamine pyrophosphate 1 is an essential cofactor in all living systems. Its biosynthesis involves the separate syntheses of the pyrimidine 2 and thiazole 3 precursors, which are then coupled. Two biosynthetic routes to the thiamine thiazole have been identified. In prokaryotes, five enzymes act on three substrates to produce the thiazole via a complex oxidative condensation reaction, the mechanistic details of which are now well established. In contrast, only one gene product is involved in thiazole biosynthesis in eukaryotes (THI4p in Saccharomyces cerevisiae). Here we report the preparation of fully active recombinant wild-type THI4p, the identification of an iron-dependent sulphide transfer reaction from a conserved cysteine residue of the protein to a reaction intermediate and the demonstration that THI4p is a suicide enzyme undergoing only a single turnover.

PubMed: 22031445
DOI: 10.1038/nature10503

Experimental method

X-RAY DIFFRACTION (1.82 Å)