1AZH

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

1AZH の概要

• エントリーDOI: 10.2210/pdb1azh/pdb
• 分子名称: CELLOBIOHYDROLASE I (1 entity in total)
• 機能のキーワード: cellulase, nuclear magnetic resonance spectroscopy, protein-carbohydrate interaction
• 由来する生物種: Hypocrea jecorina
• 細胞内の位置: Secreted: P62694
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3654.03

構造登録者

Mattinen, M.-L. (登録日: 1997-11-18, 公開日: 1998-04-08, 最終更新日: 2021-11-03)

主引用文献

Mattinen, M.L.,Kontteli, M.,Kerovuo, J.,Linder, M.,Annila, A.,Lindeberg, G.,Reinikainen, T.,Drakenberg, T.
Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Protein Sci., 6:294-303, 1997

PubMed Abstract: Three-dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel beta-sheet structure of the CBD fold was preserved in all engineered peptides. The three-dimensional NMR-based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N-terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

PubMed: 9041630

実験手法

SOLUTION NMR