Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution.

@article{Jrgensen2008SmallAX,
  title={Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution.},
  author={Anders Dysted J\orgensen and Jane N\ohr and Jette Sandholm Kastrup and Michael Gajhede and Bent W. Sigurskjold and J\orgen Sauer and Dmitri I. Svergun and Birte Svensson and Bente Vestergaard},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 21},
  pages={14772-80}
}
The industrially important glucoamylase 1 is an exo-acting glycosidase with substrate preference for alpha-1,4 and alpha-1,6 linkages at non-reducing ends of starch. It consists of a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker. The linker function is poorly understood and structurally undescribed, and data regarding domain organization and intramolecular functional cooperativity are conflicting or non-comprehensive. Here, we report a combined… CONTINUE READING