Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD
| Autor: | Xiaoming Tu, Jiahai Zhang, Hongbin Sun, Xinxin Li, Wei Zhang, Xuecheng Zhang, Jigang Yu, Hui Peng |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein Folding Circular dichroism Binding Sites Chemistry Starch beta-Cyclodextrins General Medicine SBDS Intrinsic fluorescence Ligands Biochemistry Molten globule 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology Protein Domains Structural Biology Biophysics Free form Carbohydrate-binding module alpha-Amylases Protein Binding Starch binding |
| Zdroj: | Protein & Peptide Letters. 25:362-367 |
| ISSN: | 0929-8665 |
| DOI: | 10.2174/0929866525666180122145846 |
| Popis: | AmyP is an α-amylase which shows preferential degradation to soluble starch. In this substrate preference its Starch Binding Domain (SBD), which was recently assigned to a new Carbohydrate Binding Module (CBM) family 69, plays an important role. In the present study, the SBD of AmyP (AmyP-SBD) was recombinantly expressed, purified, and structurally characterized. Using Circular Dichroism (CD), intrinsic fluorescence, and nuclear magnetic resonance (NMR) spectroscopy, the structures of AmyP-SBD in the absence and presence of substrate analogue β-cyclodextrin were measured. The results intriguingly showed that free form AmyP-SBD is partially unfolded, like a compact molten globule, and could be induced by the ligand to fold into a relatively rigid state. Further structure determination for folded AmyP-SBD revealed a topology distinctive from those of SBDs from other CBM families. Our data indicate AmyP-SBD is a structurally novel SBD, and this may be helpful for understanding the properties of AmyP-SBD and CBM69 and elucidation of functioning mechanism of AmyP. |
| Databáze: | OpenAIRE |
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