1FOB

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K

1FOB の概要

• エントリーDOI: 10.2210/pdb1fob/pdb
• 関連するPDBエントリー: 1FHL
• 分子名称: BETA-1,4-GALACTANASE, CALCIUM ION (3 entities in total)
• 機能のキーワード: b/a barrel, glycosyl hydrolase, family 53, clan gh-a, hydrolase
• 由来する生物種: Aspergillus aculeatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36815.52

構造登録者

Ryttersgaard, C.,Larsen, S. (登録日: 2000-08-27, 公開日: 2003-06-03, 最終更新日: 2024-10-16)

主引用文献

Ryttersgaard, C.,Leggio, L.L.,Coutinho, P.M.,Henrissat, B.,Larsen, S.
Aspergillus aculeatus beta-1,4-Galactanase: Substrate Recognition and Relations to Other Glycoside Hydrolases in Clan GH-A
Biochemistry, 41:15135-15143, 2002

PubMed Abstract: The three-dimensional structure of Aspergillus aculeatus beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A resolution at 293 and 100 K, respectively. It represents the first known structure for a polysaccharidase with this specificity and for a member of glycoside hydrolase family 53 (GH-53). The enzyme folds into a (beta/alpha)(8) barrel with the active site cleft located at the C-terminal side of the barrel consistent with the classification of GH-53 in clan GH-A, a superfamily of enzymes with common fold and catalytic machinery but diverse specificities. Putative substrate-enzyme interactions were elucidated by modeling of beta-1,4-linked galactobioses into the possible substrate binding subsites. The structure and modeling studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain in arabinogalactan, one of the natural substrates. A comparison with the substrate binding grooves of other Clan GH-A enzymes suggests that shape complementarity is crucial in determining the specificity of polysaccharidases.

PubMed: 12484750
DOI: 10.1021/bi026238c

実験手法

X-RAY DIFFRACTION (1.8 Å)