2KDC

NMR Solution Structure of E. coli diacylglycerol kinase (DAGK) in DPC micelles

Summary for 2KDC

• Entry DOI: 10.2210/pdb2kdc/pdb
• Descriptor: Diacylglycerol kinase (1 entity in total)
• Functional Keywords: membrane protein, kinase, dagk, cell inner membrane, cell membrane, membrane, phospholipid biosynthesis, transferase, transmembrane
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0ABN1
• Total number of polymer chains: 3
• Total formula weight: 39373.26

Authors

Van Horn, W.D.,Kim, H.,Ellis, C.D.,Hadziselimovic, A.,Sulistijo, E.S.,Karra, M.D.,Tian, C.,Sonnichsen, F.D.,Sanders, C.R. (deposition date: 2009-01-06, release date: 2009-07-07, Last modification date: 2024-05-22)

Primary citation

Van Horn, W.D.,Kim, H.J.,Ellis, C.D.,Hadziselimovic, A.,Sulistijo, E.S.,Karra, M.D.,Tian, C.,Sonnichsen, F.D.,Sanders, C.R.
Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase
Science, 324:1726-1729, 2009

PubMed Abstract: Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.

PubMed: 19556511
DOI: 10.1126/science.1171716

Experimental method

SOLUTION NMR