2LS6

Solution NMR Structure of a Non-canonical galactose-binding CBM32 from Clostridium perfringens

2LS6 の概要

• エントリーDOI: 10.2210/pdb2ls6/pdb
• NMR情報: BMRB: 17694
• 分子名称: Hyaluronoglucosaminidase (1 entity in total)
• 機能のキーワード: glycoside hydrolases, carbohyrate-binding modules, galactose, hydrolase
• 由来する生物種: Clostridium perfringens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18352.35

構造登録者

Grondin, J.M.,Chitayat, S.,Ficko-Blean, E.,Boraston, A.B.,Smith, S.P. (登録日: 2012-04-20, 公開日: 2013-05-01, 最終更新日: 2024-05-01)

主引用文献

Grondin, J.M.,Chitayat, S.,Ficko-Blean, E.,Houliston, S.,Arrowsmith, C.H.,Boraston, A.B.,Smith, S.P.
An unusual mode of galactose recognition by a family 32 carbohydrate-binding module.
J.Mol.Biol., 426:869-880, 2014

PubMed Abstract: Carbohydrate-binding modules (CBMs) are ancillary modules commonly associated with carbohydrate-active enzymes (CAZymes) that function to mediate the adherence of the parent enzyme to its carbohydrate substrates. CBM family 32 (CBM32) is one of the most diverse CBM families, whose members are commonly found in bacterial CAZymes that modify eukaryotic glycans. One such example is the putative μ-toxin, CpGH84A, of the family 84 glycoside hydrolases, which comprises an N-terminal putative β-N-acetylglucosaminidase catalytic module and four tandem CBM32s. Here, we report a unique mode of galactose recognition by the first CBM32, CBM32-1 from CpGH84A. Solution NMR-based analyses of CpGH84A CBM32-1 indicate a divergent subset of residues, located in ordered loops at the apex of the CBM, conferring specificity for the galacto-configured sugars galactose, GalNAc, and LacNAc that differs from those of the canonical galactose-binding CBM32s. This study showcases the impressive variability in ligand binding by this CBM family and offers insight into the growing role of these modules in the interaction of CAZymes with eukaryotic glycans.

PubMed: 24326248
DOI: 10.1016/j.jmb.2013.11.029

実験手法

SOLUTION NMR