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.

Search for more literature for 1.3.7.11

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	-	-

Subunits

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

Synonyms

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

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Release 2023.1 (January 2023)