4Y6N

Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-1

4Y6N の概要

• エントリーDOI: 10.2210/pdb4y6n/pdb
• 分子名称: Glucosyl-3-phosphoglycerate synthase, MANGANESE (II) ION, 3-PHOSPHOGLYCERIC ACID, ... (6 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35614.99

構造登録者

Albesa-Jove, D.,Rodrigo-Unzueta, A.,Cifuente, J.O.,Urresti, S.,Comino, N.,Sancho-Vaello, E.,Guerin, M.E. (登録日: 2015-02-13, 公開日: 2015-07-15, 最終更新日: 2024-01-10)

主引用文献

Albesa-Jove, D.,Mendoza, F.,Rodrigo-Unzueta, A.,Gomollon-Bel, F.,Cifuente, J.O.,Urresti, S.,Comino, N.,Gomez, H.,Romero-Garcia, J.,Lluch, J.M.,Sancho-Vaello, E.,Biarnes, X.,Planas, A.,Merino, P.,Masgrau, L.,Guerin, M.E.
A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase.
Angew.Chem.Int.Ed.Engl., 54:9898-9902, 2015

PubMed Abstract: Glycosyltransferases (GTs) comprise a prominent family of enzymes that play critical roles in a variety of cellular processes, including cell signaling, cell development, and host-pathogen interactions. Glycosyl transfer can proceed with either inversion or retention of the anomeric configuration with respect to the reaction substrates and products. The elucidation of the catalytic mechanism of retaining GTs remains a major challenge. A native ternary complex of a GT in a productive mode for catalysis is reported, that of the retaining glucosyl-3-phosphoglycerate synthase GpgS from M. tuberculosis in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor. Through a combination of structural, chemical, enzymatic, molecular dynamics, and quantum-mechanics/molecular-mechanics (QM/MM) calculations, the catalytic mechanism was unraveled, thereby providing a strong experimental support for a front-side substrate-assisted SN i-type reaction.

PubMed: 26136334
DOI: 10.1002/anie.201504617

実験手法

X-RAY DIFFRACTION (2.348 Å)