2AJT

Crystal structure of L-Arabinose Isomerase from E.coli

2AJT の概要

• エントリーDOI: 10.2210/pdb2ajt/pdb
• 関連するPDBエントリー: 1FUI
• 分子名称: L-arabinose isomerase (2 entities in total)
• 機能のキーワード: isomerase, arabinose catabolism, carbohydrate metabolism, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 168329.08

構造登録者

Manjasetty, B.A.,Fedorov, E.V.,Almo, S.C.,Chance, M.R.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2005-08-02, 公開日: 2005-08-16, 最終更新日: 2024-02-14)

主引用文献

Manjasetty, B.A.,Chance, M.R.
Crystal Structure of Escherichia coli L-Arabinose Isomerase (ECAI), The Putative Target of Biological Tagatose Production
J.Mol.Biol., 360:297-309, 2006

PubMed Abstract: Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.

PubMed: 16756997
DOI: 10.1016/j.jmb.2006.04.040

実験手法

X-RAY DIFFRACTION (2.6 Å)