3WN0

Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with L-arabinose

3WN0 の概要

• エントリーDOI: 10.2210/pdb3wn0/pdb
• 関連するPDBエントリー: 3WMY 3WMZ 3WN1 3WN2
• 分子名称: Extracellular exo-alpha-L-arabinofuranosidase, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: five-bladed beta-propeller, glycoside hydrolase, hydrolase
• 由来する生物種: Streptomyces coelicolor
• 細胞内の位置: Secreted : O54161
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46941.86

構造登録者

Fujimoto, Z.,Maehara, T.,Ichinose, H.,Michikawa, M.,Harazono, K.,Kaneko, S. (登録日: 2013-11-29, 公開日: 2014-02-05, 最終更新日: 2024-11-06)

主引用文献

Maehara, T.,Fujimoto, Z.,Ichinose, H.,Michikawa, M.,Harazono, K.,Kaneko, S.
Crystal structure and characterization of the glycoside hydrolase family 62 alpha-L-arabinofuranosidase from Streptomyces coelicolor
J.Biol.Chem., 289:7962-7972, 2014

PubMed Abstract: α-L-arabinofuranosidase, which belongs to the glycoside hydrolase family 62 (GH62), hydrolyzes arabinoxylan but not arabinan or arabinogalactan. The crystal structures of several α-L-arabinofuranosidases have been determined, although the structures, catalytic mechanisms, and substrate specificities of GH62 enzymes remain unclear. To evaluate the substrate specificity of a GH62 enzyme, we determined the crystal structure of α-L-arabinofuranosidase, which comprises a carbohydrate-binding module family 13 domain at its N terminus and a catalytic domain at its C terminus, from Streptomyces coelicolor. The catalytic domain was a five-bladed β-propeller consisting of five radially oriented anti-parallel β-sheets. Sugar complex structures with l-arabinose, xylotriose, and xylohexaose revealed five subsites in the catalytic cleft and an l-arabinose-binding pocket at the bottom of the cleft. The entire structure of this GH62 family enzyme was very similar to that of glycoside hydrolase 43 family enzymes, and the catalytically important acidic residues found in family 43 enzymes were conserved in GH62. Mutagenesis studies revealed that Asp(202) and Glu(361) were catalytic residues, and Trp(270), Tyr(461), and Asn(462) were involved in the substrate-binding site for discriminating the substrate structures. In particular, hydrogen bonding between Asn(462) and xylose at the nonreducing end subsite +2 was important for the higher activity of substituted arabinofuranosyl residues than that for terminal arabinofuranoses.

PubMed: 24482228
DOI: 10.1074/jbc.M113.540542

実験手法

X-RAY DIFFRACTION (1.9 Å)