1A3X
PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+
Summary for 1A3X
| Entry DOI | 10.2210/pdb1a3x/pdb |
| Descriptor | PYRUVATE KINASE, 2-PHOSPHOGLYCOLIC ACID, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | pyruvate kinase, allosteric regulation, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 109725.02 |
| Authors | Jurica, M.S.,Mesecar, A.,Heath, P.J.,Shi, W.,Nowak, T.,Stoddard, B.L. (deposition date: 1998-01-26, release date: 1998-05-27, Last modification date: 2024-12-25) |
| Primary citation | Jurica, M.S.,Mesecar, A.,Heath, P.J.,Shi, W.,Nowak, T.,Stoddard, B.L. The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate. Structure, 6:195-210, 1998 Cited by PubMed Abstract: Yeast pyruvate kinase (PK) catalyzes the final step in glycolysis. The enzyme therefore represents an important control point and is allosterically activated by fructose-1,6-bisphosphate (FBP). In mammals the enzyme is found as four different isozymes with different regulatory properties: two of these isozymes are produced by alternate splicing. The allosteric regulation of PK is directly related to proliferation of certain cell types, as demonstrated by the expression of an allosterically regulated isozyme in tumor cells. A model for the allosteric transition from the inactive (T) state to the active (R) state has been proposed previously, but until now the FBP-binding site had not been identified. PubMed: 9519410DOI: 10.1016/S0969-2126(98)00021-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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