Summary for 3R1X
| Entry DOI | 10.2210/pdb3r1x/pdb |
| Descriptor | 2-oxo-3-deoxygalactonate kinase, FORMIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | structural genomics, psi-biology, midwest center for structural genomics, mcsg, 2-oxo-3-deoxygalactonate kinase, 2-dehydro-3-deoxygalactonokinase, 2-keto-3-deoxygalactonate kinase, deley-doudoroff pathway, transferase |
| Biological source | Klebsiella pneumoniae subsp. pneumoniae |
| Total number of polymer chains | 4 |
| Total formula weight | 128442.01 |
| Authors | Michalska, K.,Cuff, M.E.,Tesar, C.,Feldmann, B.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2011-03-11, release date: 2011-04-13, Last modification date: 2011-09-21) |
| Primary citation | Michalska, K.,Cuff, M.E.,Tesar, C.,Feldmann, B.,Joachimiak, A. Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae. Acta Crystallogr.,Sect.D, 67:678-689, 2011 Cited by PubMed Abstract: In most organisms, efficient D-galactose utilization requires the highly conserved Leloir pathway that converts D-galactose to D-glucose 1-phosphate. However, in some bacterial and fungal species alternative routes of D-galactose assimilation have been identified. In the so-called De Ley-Doudoroff pathway, D-galactose is metabolized into pyruvate and D-glyceraldehyde 3-phosphate in five consecutive reactions carried out by specific enzymes. The penultimate step in this pathway involves the phosphorylation of 2-oxo-3-deoxygalactonate to 2-oxo-3-deoxygalactonate 6-phosphate catalyzed by 2-oxo-3-deoxygalactonate kinase, with ATP serving as a phosphoryl-group donor. Here, a crystal structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae determined at 2.1 Å resolution is reported, the first structure of an enzyme from the De Ley-Doudoroff pathway. Structural comparison indicates that the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases. The protein is composed of two α/β domains, each of which contains a core common to all family members. Additional elements introduced between conserved structural motifs define the unique features of 2-oxo-3-deoxygalactonate kinase and possibly determine the biological function of the protein. PubMed: 21795809DOI: 10.1107/S0907444911021834 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.093 Å) |
Structure validation
Download full validation report
