Thermoplasma acidophilum

vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid

Thermoplasma acidophilum

2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+

Thermoplasma acidophilum

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+

?

Thermoplasma acidophilum

Q9HKS9

Thermoplasma acidophilum

2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

712772

Thermoplasma acidophilum

2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+

?

2,3-digeranylgeranylglycerophospholipid reductase

Thermoplasma acidophilum

digeranylgeranylglycerophospholipid reductase

Thermoplasma acidophilum

FAD

the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD

Thermoplasma acidophilum

Thermoplasma acidophilum

FAD

the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD

Thermoplasma acidophilum

vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid

Thermoplasma acidophilum

2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+

Thermoplasma acidophilum

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+

?

Thermoplasma acidophilum

2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

712772

Thermoplasma acidophilum

2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+

?

physiological function

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

Thermoplasma acidophilum

physiological function

the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions

Thermoplasma acidophilum

719041

Nishimura

Stereochemistry of reduction i ...

Bioorg. Chem.

719758

Nishimura

Biosynthesis of archaeal membr ...

J. Biochem.