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Protein Pept Lett. 2018;25(4):362-367. doi: 10.2174/0929866525666180122145846.

Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD.

Author information

1
School of Life Sciences, Anhui University, Hefei, Anhui 230601, China.
2
Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
3
High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Academy of Sciences of China, Hefei 230031, China.

Abstract

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.

KEYWORDS:

AmyP; Starch binding domain; carbohydrate binding module family 69; ligand induced folding; molten globule; nuclear magnetic resonance.

[Indexed for MEDLINE]

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