Literature summary for 2.7.7.70 extracted from

Park, J.; Kim, H.; Kim, S.; Lee, D.; Shin, D.H.
Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei (2017), Acta Crystallogr. Sect. F, 73, 90-94 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene hldC, recombinant expression of noncleavably N-terminally His6-tagged SeMet-labeled BpHldC in Escherichia coli strain B834(DE3)	Burkholderia pseudomallei

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified SeMet-labeled enzyme containing a noncleavable N-terminal His6-tag, hanging drop vapour diffusion method, mixing of 800 nl of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 0.35 M NaCl with 800 nl of reservoir solution containing 0.1 M HEPES, pH 7.0, 20% w/v PEG 3350, and 8.5 mM n-octyl-beta-D-thiomaltoside, and equilibration over 0.05 ml of reservoir solution, room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.80 A resolution, rod-shaped crystals, automated model building	Burkholderia pseudomallei

Crystallization (Comment)

Organism

purified SeMet-labeled enzyme containing a noncleavable N-terminal His6-tag, hanging drop vapour diffusion method, mixing of 800 nl of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 0.35 M NaCl with 800 nl of reservoir solution containing 0.1 M HEPES, pH 7.0, 20% w/v PEG 3350, and 8.5 mM n-octyl-beta-D-thiomaltoside, and equilibration over 0.05 ml of reservoir solution, room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.80 A resolution, rod-shaped crystals, automated model building

Burkholderia pseudomallei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Burkholderia pseudomallei

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glycero-beta-D-manno-heptose 1-phosphate + ATP	Burkholderia pseudomallei	-	ADP-D-glycero-beta-D-manno-heptose + diphosphate	-	?
D-glycero-beta-D-manno-heptose 1-phosphate + ATP	Burkholderia pseudomallei K96243	-	ADP-D-glycero-beta-D-manno-heptose + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Burkholderia pseudomallei	Q63XZ4	-	-
Burkholderia pseudomallei K96243	Q63XZ4	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His6-tagged SeMet-labeled BpHldC from Escherichia coli strain B834(DE3) by nickel affinity and anion exchange chromatography to about 99% purity	Burkholderia pseudomallei

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glycero-beta-D-manno-heptose 1-phosphate + ATP	-	Burkholderia pseudomallei	ADP-D-glycero-beta-D-manno-heptose + diphosphate	-	?
D-glycero-beta-D-manno-heptose 1-phosphate + ATP	-	Burkholderia pseudomallei K96243	ADP-D-glycero-beta-D-manno-heptose + diphosphate	-	?

Subunits

Subunits	Comment	Organism
?	x * 19000, recombinant His6-tagged SeMet-labeled enzyme, SDS-PAGE	Burkholderia pseudomallei

Synonyms

Synonyms	Comment	Organism
D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase	-	Burkholderia pseudomallei
HldC	-	Burkholderia pseudomallei

General Information

General Information	Comment	Organism
metabolism	D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-1-glycero-beta-D-manno-heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide	Burkholderia pseudomallei