Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
D138A | point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity | Aquifex aeolicus |
D139A | point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity | Aquifex aeolicus |
G47A | about 43% of wild-type activity | Aquifex aeolicus |
G48A | about 1.8% of wild-type activity | Aquifex aeolicus |
G50A | about 0.1% of wild-type activity | Aquifex aeolicus |
K51A | about 0.1% of wild-type activity | Aquifex aeolicus |
S53A | about 9.9% of wild-type activity | Aquifex aeolicus |
T52A | about 0.1% of wild-type activity | Aquifex aeolicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | O67572 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
LpxK | - |
Aquifex aeolicus |