2UYT
Structure of L-rhamnulose kinase in complex with ADP and beta-L- rhamnulose.
Summary for 2UYT
| Entry DOI | 10.2210/pdb2uyt/pdb |
| Related | 2CGJ 2CGK 2CGL |
| Descriptor | RHAMNULOKINASE, 6-deoxy-beta-L-fructofuranose, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | rhamnose degradation, in-line phosphoryl transfer, hexokinase-hsp70-actin superfamily, l-rhamnulose kinase, rhamnose metabolism, kinase, induced fit, transferase, rare sugars |
| Biological source | ESCHERICHIA COLI BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 54546.07 |
| Authors | Grueninger, D.,Schulz, G.E. (deposition date: 2007-04-13, release date: 2007-06-26, Last modification date: 2024-10-09) |
| Primary citation | Grueninger, D.,Schulz, G.E. Substrate Spectrum of L-Rhamnulose Kinase Related to Models Derived from Two Ternary Complex Structures. FEBS Lett., 581:3127-, 2007 Cited by PubMed Abstract: The enzyme L-rhamnulose kinase from Escherichia coli participates in the degradation pathway of L-rhamnose, a common natural deoxy-hexose. The structure of the enzyme in a ternary complex with its substrates ADP and L-rhamnulose has been determined at 1.55A resolution and refined to R(cryst)/R(free) values of 0.179/0.209. The result was compared with the lower resolution structure of a corresponding complex containing L-fructose instead of L-rhamnulose. In light of the two established sugar positions and conformations, a number of rare sugars have been modeled into the active center of L-rhamnulose kinase and the model structures have been compared with the known enzymatic phosphorylation rates. Rare sugars are of rising interest for the synthesis of bioactive compounds. PubMed: 17568582DOI: 10.1016/J.FEBSLET.2007.05.075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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