| Autor: |
Einsle, Oliver, Niessen, Holger, Abt, Dietmar J., Seiffert, Grazyna, Schink, Bernhard, Huber, Robert, Messerschmid, Albrecht, Kroneck, Peter M. H. |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section F (Wiley-Blackwell); Mar2005, Vol. 61 Issue 3, p302-304, 3p |
| Abstrakt: |
A maltooligosaccharide-metabolizing enzyme from Thermoactinomyces vulgaris R-47 (TGA) homologous to glucoamylase degrades maltooligosacchar-ides more efficiently than starch, unlike fungal glucoamylases. TGA was crystallized and the state of the protein in solution was analyzed by gel-filtration chromatography. Diffraction data were collected to 3.31 Å resolution. The TGA crystal belongs to the orthorhombic space group P212121 or P21212, with unit-cell parameters a = 110.2, b = 317.6, c = 144.9 Å, and is expected to contain five to eight TGA molecules per asymmetric unit. Gel-filtration and native PAGE analyses indicated that TGA exists as a dimer in solution. This is the first report of the crystallization of an oligomeric glucoamylase. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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