3EQA

Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

Summary for 3EQA

• Entry DOI: 10.2210/pdb3eqa/pdb
• Descriptor: Glucoamylase, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: hydrolase, glycoprotein, glycosidase, polysaccharide degradation
• Biological source: Aspergillus Niger
• Total number of polymer chains: 1
• Total formula weight: 54122.08

Authors

Lee, J.,Paetzel, M. (deposition date: 2008-09-30, release date: 2009-10-13, Last modification date: 2024-10-30)

Primary citation

Lee, J.,Paetzel, M.
Structure of the catalytic domain of glucoamylase from Aspergillus niger.
Acta Crystallogr.,Sect.F, 67:188-192, 2011

PubMed Abstract: Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been crystallized at pH 8.5, which is a significantly higher pH condition than used for previously characterized glucoamylase crystals. The refined structure at 1.9 Å resolution reveals the active site of the enzyme in complex with both Tris and glycerol molecules. The ligands display both unique and analogous interactions with the substrate-binding site when compared with previous structures of homologous enzymes bound to inhibitors.

PubMed: 21301084
DOI: 10.1107/S1744309110049390

Experimental method

X-RAY DIFFRACTION (1.9 Å)