Literature summary extracted from
Emptage, R.P.; Daughtry, K.D.; Pemble, C.W.; Raetz, C.R.
Crystal structure of LpxK, the 4-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface (2012), Proc. Natl. Acad. Sci. USA, 109, 12956-12961.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.1.130 |
apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base |
Aquifex aeolicus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.1.130 |
D138A |
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
D139A |
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
G47A |
about 43% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
G48A |
about 1.8% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
G50A |
about 0.1% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
K51A |
about 0.1% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
S53A |
about 9.9% of wild-type activity |
Aquifex aeolicus |
2.7.1.130 |
T52A |
about 0.1% of wild-type activity |
Aquifex aeolicus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.1.130 |
Aquifex aeolicus |
O67572 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.1.130 |
LpxK |
- |
Aquifex aeolicus |