2ZUT

Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc

2ZUT の概要

• エントリーDOI: 10.2210/pdb2zut/pdb
• 関連するPDBエントリー: 2ZUS 2ZUU 2ZUV 2ZUW
• 分子名称: Lacto-N-biose phosphorylase, 2-acetamido-2-deoxy-alpha-D-galactopyranose, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: beta-alpha-barrel, tim barrel, glycosyltransferase, transferase
• 由来する生物種: Bifidobacterium longum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 343857.76

構造登録者

Hidaka, M.,Nishimoto, M.,Kitaoka, M.,Wakagi, T.,Shoun, H.,Fushinobu, S. (登録日: 2008-10-28, 公開日: 2008-12-30, 最終更新日: 2024-03-13)

主引用文献

Hidaka, M.,Nishimoto, M.,Kitaoka, M.,Wakagi, T.,Shoun, H.,Fushinobu, S.
The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: A large deformation of a tim barrel scaffold
J.Biol.Chem., 284:7273-7283, 2009

PubMed Abstract: Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) from Bifidobacterium longum, a key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc- and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic beta-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates.

PubMed: 19124470
DOI: 10.1074/jbc.M808525200

実験手法

X-RAY DIFFRACTION (1.9 Å)