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Literature summary for 2.7.1.107 extracted from

  • Miller, D.J.; Jerga, A.; Rock, C.O.; White, S.W.
    Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases (2008), Structure, 16, 1036-1046.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
isoform DgkB, both as free enzyme and in complex with ADP, 2.4 and 2.3 A resolution, respectively. Enzyme is a tight homodimer, and each monomer comprises two domains with the catalytic center located within the interdomain cleft Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
D124A residue involved in the Mg1-water network, no catalytic acitivity Staphylococcus aureus
D271A residue involved in the Mg1-water network, no catalytic acitivity Staphylococcus aureus
D68A no catalytic activity. Role of D68 in mediating the interaction of Mg2+ with the gamma-phosphate of ATP Staphylococcus aureus
E273A no catalytic activity Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ structure reveals a Mg2+ site and an associated Asp-water-Mg2+ network Staphylococcus aureus
additional information neither Ca2+, Mn2+, nor Zn2+ is able to effectively replace Mg2+, although Ca2+ and Mn2+ support a few percent activity Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37333
-
 x * 37333, calculated, x * 42000, SDS-PAGE Staphylococcus aureus
42000
-
 x * 37333, calculated, x * 42000, SDS-PAGE Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q6GFF9
-
-

Subunits

Subunits Comment Organism
? x * 37333, calculated, x * 42000, SDS-PAGE Staphylococcus aureus