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Literature summary extracted from

  • Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Duine, J.A.; Dijkstra, B.W.
    The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat (1999), J. Mol. Biol., 289, 319-333.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.5.2 apo form of the soluble glucose dehydrogenase Acinetobacter calcoaceticus
1.1.99.35 at 1.72 A resolution. The s-GDH monomer has a beta-propeller fold consisting of six four-stranded anti-parallel beta-sheets aligned around a pseudo 6-fold symmetry axis. The enzyme binds three calcium ions per monomer, two of which are located in the dimer interface. The third is bound in the putative active site, where it may bind and functionalize the pyrroloquinoline quinone cofactor Acinetobacter calcoaceticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.35 Ca2+ the enzyme binds three calcium ions per monomer, two of which are located in the dimer interface, crystallization data Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Acinetobacter calcoaceticus P13650
-
-
1.1.99.35 Acinetobacter calcoaceticus P13650
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.35 pyrroloquinoline quinone crystallization data Acinetobacter calcoaceticus