3AI7
Crystal Structure of Bifidobacterium Longum Phosphoketolase
Summary for 3AI7
| Entry DOI | 10.2210/pdb3ai7/pdb |
| Descriptor | Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase, THIAMINE DIPHOSPHATE, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | thiamine-diphosphate protein, lyase |
| Biological source | Bifidobacterium longum |
| Total number of polymer chains | 8 |
| Total formula weight | 751323.26 |
| Authors | Takahashi, K.,Tagami, U.,Shimba, N.,Kashiwagi, T.,Ishikawa, K.,Suzuki, E. (deposition date: 2010-05-10, release date: 2010-09-15, Last modification date: 2024-04-03) |
| Primary citation | Takahashi, K.,Tagami, U.,Shimba, N.,Kashiwagi, T.,Ishikawa, K.,Suzuki, E. Crystal structure of Bifidobacterium Longum phosphoketolase; key enzyme for glucose metabolism in Bifidobacterium Febs Lett., 584:3855-3861, 2010 Cited by PubMed Abstract: The crystal structure of Bifidobacterium longum phosphoketolase, a thiamine diphosphate (TPP) dependent enzyme, has been determined at 2.2A resolution. The enzyme is a dimer with the active sites located at the interface between the two identical subunits with molecular mass of 92.5 kDa. The bound TPP is almost completely shielded from solvent except for the catalytically important C2-carbon of the thiazolium ring, which can be accessed by a substrate sugar through a narrow funnel-shaped channel. In silico docking studies of B. longum phosphoketolase with its substrate enable us to propose a model for substrate binding. PubMed: 20674574DOI: 10.1016/j.febslet.2010.07.043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
