2INV

Crystal structure of Inulin fructotransferase in the presence of di-fructose

2INV の概要

• エントリーDOI: 10.2210/pdb2inv/pdb
• 関連するPDBエントリー: 2INU
• 分子名称: Inulin fructotransferase, beta-D-fructofuranose-(2-1)-beta-D-fructofuranose, PHOSPHONATE, ... (4 entities in total)
• 機能のキーワード: right-handed parallel beta-helix, protein-carbohydrate complex, lyase
• 由来する生物種: Bacillus sp. snu-7
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 131977.41

構造登録者

Rhee, S.,Jung, W.S. (登録日: 2006-10-09, 公開日: 2006-12-26, 最終更新日: 2024-10-16)

主引用文献

Jung, W.S.,Hong, C.K.,Lee, S.,Kim, C.S.,Kim, S.J.,Kim, S.I.,Rhee, S.
Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase
J.Biol.Chem., 282:8414-8423, 2007

PubMed Abstract: Inulin fructotransferase (IFTase), a member of glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. The crystal structures of IFTase and its substrate-bound complex reveal that IFTase is a trimeric enzyme, and each monomer folds into a right-handed parallel beta-helix. Despite variation in the number and conformation of its beta-strands, the IFTase beta-helix has a structure that is largely reminiscent of other beta-helix structures but is unprecedented in that trimerization is a prerequisite for catalytic activity, and the active site is located at the monomer-monomer interface. Results from crystallographic studies and site-directed mutagenesis provide a structural basis for the exolytic-type activity of IFTase and a functional resemblance to inverting-type glycosyltransferases.

PubMed: 17192265
DOI: 10.1074/jbc.M607143200

実験手法

X-RAY DIFFRACTION (1.8 Å)