1IIM

thymidylyltransferase complexed with TTP

1IIM の概要

• エントリーDOI: 10.2210/pdb1iim/pdb
• 関連するPDBエントリー: 1IIN 1MP3 1MP4 1MP5
• 分子名称: glucose-1-phosphate thymidylyltransferase, THYMIDINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Salmonella enterica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66899.07

構造登録者

Barton, W.A.,Lesniak, J.,Biggins, J.B.,Jeffrey, P.D.,Jiang, J.,Rajashankar, K.R.,Thorson, J.S.,Nikolov, D.B. (登録日: 2001-04-23, 公開日: 2001-05-09, 最終更新日: 2024-02-07)

主引用文献

Barton, W.A.,Lesniak, J.,Biggins, J.B.,Jeffrey, P.D.,Jiang, J.,Rajashankar, K.R.,Thorson, J.S.,Nikolov, D.B.
Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization.
Nat.Struct.Biol., 8:545-551, 2001

PubMed Abstract: Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.

PubMed: 11373625
DOI: 10.1038/88618

実験手法

X-RAY DIFFRACTION (2.1 Å)