4EIB

Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.

4EIB の概要

• エントリーDOI: 10.2210/pdb4eib/pdb
• 分子名称: Glucoamylase, SULFATE ION, AMMONIUM ION, ... (7 entities in total)
• 機能のキーワード: beta barrel, starch binding, amylose, hydrolase
• 由来する生物種: Rhizopus oryzae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25464.22

構造登録者

Stephen, P.,Cheng, K.C.,Lyu, P.C. (登録日: 2012-04-05, 公開日: 2012-12-12, 最終更新日: 2023-11-08)

主引用文献

Stephen, P.,Cheng, K.C.,Lyu, P.C.
Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites
Plos One, 7:e50488-e50488, 2012

PubMed Abstract: Glucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their ligands, whereas circular permutation of the RoCBM21 substantially improved its binding affinity and selectivity towards longer-chain carbohydrates. For the study reported herein, we used a standard soluble ligand (amylose EX-I) to characterize the functional and structural aspects of circularly permuted RoCBM21 (CP90). Site-directed mutagenesis and the analysis of crystal structure reveal the dimerisation and an altered binding path, which may be responsible for improved affinity and altered selectivity of this newly created starch-binding domain. The functional and structural characterization of CP90 suggests that it has significant potential in industrial applications.

PubMed: 23226294
DOI: 10.1371/journal.pone.0050488

実験手法

X-RAY DIFFRACTION (1.86 Å)