Crystallization (Comment) | Organism |
---|---|
purified recombinanz wild-type and DELTA4 and DELTA7 mutant enzymes in complex with lipid substrate and ATP, 20°C, X-ray diffraction structure determination and analysis at 2.05 A resolution, structure mmodeling. The kinase adopts a functional form in the crystal. Domain swapping, a key feature of the solution form, is not observed in the crystal structures. Crystals of mutant DELTA7 DgkA are soaked with the ATP analogue, adenylylmethylenediphosphate (Mg2+-AMPPCP). This causes the crystals to dissolve. Additional soaking with ATP, ADP, AMP, ATP?S, AMPPNP and dATP but not with GTP, CTP, UTP or TTP leads to crystal dissolution | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a thermostabilized DELTA4 (4 changes relative to wild-type) form of DgkA using the DELTA7 structure, overview | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell envelope | - |
Escherichia coli | 30313 | - |
membrane | the enzyme is an integral membrane protein | Escherichia coli | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli | |
Zn2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1,2-diacyl-sn-glycerol | Escherichia coli | - |
ADP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0ABN1 | gene dgkA | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1,2-diacyl-sn-glycerol | - |
Escherichia coli | ADP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotrimer | a homotrimeric enzyme with three transmembrane helices and an N-terminal amphiphilic helix per monomer. Bound lipid substrate and docked ATP identify the putative active site which is of the composite, shared site type. Each subunit within a trimer forms a bundle of 3 transmembrane helices. The three subunits are arranged around an approximate 3-fold symmetry axis that passes through the center of the trimer normal to the membrane plane, enzyme structure analysis, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
DGKA | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | DgkA is a unique kinase with a distinctive active site. It has no recognizable nucleotide sequence or structural binding motifs | Escherichia coli |
additional information | DgkA catalyzes phosphoryl transfer expected to take place at a polar/apolar interface | Escherichia coli |
physiological function | diacylglycerol kinase catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid for use in shuttling water-soluble components to membrane-derived oligosaccharide and lipopolysaccharide in the cell envelope of Gram-negative bacteria | Escherichia coli |