2QV7
Crystal Structure of Diacylglycerol Kinase DgkB in complex with ADP and Mg
Summary for 2QV7
Entry DOI | 10.2210/pdb2qv7/pdb |
Related | 2QVL |
Descriptor | Diacylglycerol Kinase DgkB, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | alpha-beta domain 1, beta sandwich domain 2, protein-adp complex, transferase |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 1 |
Total formula weight | 38350.74 |
Authors | Miller, D.J.,Jerga, A.,Rock, C.O.,White, S.W. (deposition date: 2007-08-07, release date: 2008-06-17, Last modification date: 2011-07-13) |
Primary citation | 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. Structure, 16:1036-1046, 2008 Cited by PubMed Abstract: Soluble diacylglycerol (DAG) kinases function as regulators of diacylglycerol metabolism in cell signaling and intermediary metabolism. We report the structure of a DAG kinase, DgkB from Staphylococcus aureus, both as the free enzyme and in complex with ADP. The molecule is a tight homodimer, and each monomer comprises two domains with the catalytic center located within the interdomain cleft. Two distinctive features of DkgB are a structural Mg2+ site and an associated Asp*water*Mg2+ network that extends toward the active site locale. Site-directed mutagenesis revealed that these features play important roles in the catalytic mechanism. The key active site residues and the components of the Asp*water*Mg2+ network are conserved in the catalytic cores of the mammalian signaling DAG kinases, indicating that these enzymes use the same mechanism and have similar structures as DgkB. PubMed: 18611377DOI: 10.1016/j.str.2008.03.019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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