Literature summary for 2.7.8.43 extracted from

Anandan, A.; Piek, S.; Kahler, C.; Vrielink, A.
Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis (2012), Acta Crystallogr. Sect. F, 68, 1494-1497.

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged membrane-deletion mutant enzyme in Escherichia coli strain BL21(DE3)pLysS	Neisseria meningitidis

Crystallization (Commentary)

Crystallization (Comment)	Organism
recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.58.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution	Neisseria meningitidis

Crystallization (Comment)

Organism

recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.58.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution

Neisseria meningitidis

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a membrane-deletion mutant of the enzyme	Neisseria meningitidis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Neisseria meningitidis	-	-

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	Q7DDQ9	gene lptA	-
Neisseria meningitidis NMB	Q7DDQ9	gene lptA	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged membrane-deletion mutant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis	Neisseria meningitidis

Subunits

Subunits	Comment	Organism
More	the enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain. Tryptic peptide mapping and analysis by MALDI-TOF/TOF mass spectrometry	Neisseria meningitidis

Synonyms

Synonyms	Comment	Organism
NmLptA	-	Neisseria meningitidis
phosphoethanolamine transferase A	-	Neisseria meningitidis

General Information

General Information	Comment	Organism
physiological function	the enzyme phosphoethanolamine transferase A is involved in the addition of phosphoethanolamine moieties to lipid A	Neisseria meningitidis