1TKC

SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE

1TKC の概要

• エントリーDOI: 10.2210/pdb1tkc/pdb
• 分子名称: TRANSKETOLASE, CALCIUM ION, 6'-METHYL-THIAMIN DIPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 148267.01

構造登録者

Schneider, G.,Koenig, S. (登録日: 1994-02-07, 公開日: 1994-11-30, 最終更新日: 2024-02-14)

主引用文献

Konig, S.,Schellenberger, A.,Neef, H.,Schneider, G.
Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate.
J.Biol.Chem., 269:10879-10882, 1994

PubMed Abstract: The three-dimensional structures of complexes of yeast apotransketolase with the coenzyme analogs 6'-methyl, N1'-pyridyl, and N3'-pyridyl thiamin diphosphate, respectively, were determined with protein crystallographic methods. All three coenzyme analogs bind to the enzyme in a fashion highly similar to the cofactor thiamin diphosphate. Thus, either one of the hydrogen bonds of the pyrimidine ring nitrogens to the protein is sufficient for proper binding and positioning of the cofactor. The lack of catalytic activity of the N3'-pyridyl analog is not due to incorrect orientation of the pyrimidine ring, but results from the absence of the hydrogen bond between the N1' nitrogen atom and the conserved residue Glu418. The structure analysis provides further evidence for the importance of this conserved interaction for enzymatic thiamin catalysis.

PubMed: 8144674

実験手法

X-RAY DIFFRACTION (2.7 Å)