3A71

High resolution structure of Penicillium chrysogenum alpha-L-arabinanase

3A71 の概要

• エントリーDOI: 10.2210/pdb3a71/pdb
• 関連するPDBエントリー: 3A72
• 分子名称: Exo-arabinanase, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: arabinase, glycosyl hydrolase, hydrolase
• 由来する生物種: Penicillium chrysogenum (Penicillium notatum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39773.19

構造登録者

Sogabe, Y. (登録日: 2009-09-11, 公開日: 2010-09-15, 最終更新日: 2024-03-13)

主引用文献

Sogabe, Y.,Kitatani, T.,Yamaguchi, A.,Kinoshita, T.,Adachi, H.,Takano, K.,Inoue, T.,Mori, Y.,Matsumura, H.,Sakamoto, T.,Tada, T.
High-resolution structure of exo-arabinanase from Penicillium chrysogenum
Acta Crystallogr.,Sect.D, 67:415-422, 2011

PubMed Abstract: Arabinanase Abnx from Penicillium chrysogenum 31B, which belongs to the GH93 family, releases arabinobiose from the nonreducing terminus of α-1,5-L-arabinan, which is distributed in the primary cell walls of higher plants. Crystal structures of Abnx and of its complex with arabinobiose were determined at the high resolutions of 1.14 Å to an R(work) of 10.7% (R(free) = 12.8%) and 1.04 Å to an R(work) of 10.4% (R(free) = 12.5%). Abnx has a six-bladed β-propeller fold with a typical ring-closure mode called `Velcro', in which the last four-stranded β-sheet is completed by the incorporation of a strand from the N-terminus. Catalytic residues which act as a nucleophile and an acid/base were proposed from the structures and confirmed by site-directed mutagenesis. The substrate-binding groove is enclosed at one end by two residues, Glu64 and Tyr66, which contribute to the recognition of the nonreducing chain end of the polysaccharide. A comparison with the related enzyme Arb93A which has a quite similar overall structure suggested that Abnx has different mechanisms to funnel substrates to the active site and/or to stabilize the transition state.

PubMed: 21543843
DOI: 10.1107/S0907444911006299

実験手法

X-RAY DIFFRACTION (1.14 Å)