ArticleActa crystallographica. Section F, Structural biology communications2017
Crystal structure of the starch-binding domain of glucoamylase from Aspergillus niger.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Crystal structure of Legionella pneumophila glycosidase effector LegY.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Novel Design of an α-Amylase with an N-Terminal CBM20 inMolecules (Basel, Switzerland) · 2023Article
- Improving Thermostability of Chimeric Enzymes Generated by Domain Shuffling Between Two Different Original Glucoamylases.Frontiers in bioengineering and biotechnology · 2022Article
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4 authors.
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Abstract
Glucoamylases are widely used commercially to produce glucose syrup from starch. The starch-binding domain (SBD) of glucoamylase from Aspergillus niger is a small globular protein containing a disulfide bond. The structure of A. niger SBD has been determined by NMR, but the conformation surrounding the disulfide bond was unclear. Therefore, X-ray crystal structural analysis was used to attempt to clarify the conformation of this region. The SBD was purified from an Escherichia coli-based expression system and crystallized at 293 K. The initial phase was determined by the molecular-replacement method, and the asymmetric unit of the crystal contained four protomers, two of which were related by a noncrystallographic twofold axis. Finally, the structure was solved at 2.0 Å resolution. The SBD consisted of seven β-strands and eight loops, and the conformation surrounding the disulfide bond was determined from a clear electron-density map. Comparison of X-ray- and NMR-determined structures of the free SBD showed no significant difference in the conformation of each β-strand, but the conformations of the loops containing the disulfide bond and the L5 loop were different. In particular, the difference in the position of the C
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