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Literature summary for 1.3.7.11 extracted from

  • Sasaki, D.; Fujihashi, M.; Iwata, Y.; Murakami, M.; Yoshimura, T.; Hemmi, H.; Miki, K.
    Structure and mutation analysis of archaeal geranylgeranyl reductase (2011), J. Mol. Biol., 409, 543-557.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sulfolobus acidocaldarius

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are obtained using 3.5-4.5 M sodium formate with 0.1 M sodium acetate buffer, pH 4.6, as the precipitant solution and 1.0 mM geranylgeranyl diphosphate is added for co-crystallization, 1.8 A resolution Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q4JA33
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Subunits

Subunits Comment Organism
monomer divided into the FADbinding, catalytic and C-terminal domains Sulfolobus acidocaldarius

Synonyms

Synonyms Comment Organism
geranylgeranyl reductase
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Sulfolobus acidocaldarius
Sa-GGR
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Sulfolobus acidocaldarius

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein, the catalytic domain has a large cavity surrounded by a characteristic YxWxFPx7-8GxG motif and by the isoalloxazine ring of an FAD molecule Sulfolobus acidocaldarius