4BF7

Emericilla nidulans endo-beta-1,4-galactanase

4BF7 の概要

• エントリーDOI: 10.2210/pdb4bf7/pdb
• 分子名称: ARABINOGALACTAN ENDO-1,4-BETA-GALACTOSIDASE A, ZINC ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
• 細胞内の位置: Secreted (By similarity): Q5B153
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40749.64

構造登録者

Otten, H.,Michalak, M.,Larsen, S.,Mikkelsen, J.D. (登録日: 2013-03-15, 公開日: 2013-08-07, 最終更新日: 2024-11-13)

主引用文献

Otten, H.,Michalak, M.,Mikkelsen, J.D.,Larsen, S.
The Binding of Zinc Ions to Emericella Nidulans Endo-[Beta]-1,4-Galactanase is Essential for Crystal Formation
Acta Crystallogr.,Sect.F, 69:850-, 2013

PubMed Abstract: A novel Emericella nidulans endo-β-1,4-galactanase (EnGAL) demonstrates a strong capacity to generate high levels of very potent prebiotic oligosaccharides from potato pulp, a by-product of the agricultural potato-starch industry. EnGAL belongs to glycoside hydrolase family 53 and shows high (72.5%) sequence identity to an endo-β-1,4-galactanase from Aspergillus aculeatus. Diffraction data extending to 2.0 Å resolution were collected from a crystal of EnGAL grown from conditions containing 0.2 M zinc acetate. The crystal structure showed a high similarity between EnGAL and other endo-β-1,4-galactanases belonging to GH53. It also revealed 15 zinc ions bound to the protein, one of which is located in the active site, where it is coordinated by residues Glu136 and Glu246 which comprise the catalytic machinery. The majority of the zinc ions are located on the surface of the enzyme, in some cases with side chains from two different molecules as ligands, thus explaining why the presence of zinc ions was essential for crystallization.

PubMed: 23908026
DOI: 10.1107/S1744309113019714

実験手法

X-RAY DIFFRACTION (2.001 Å)