2uyt | pdb_00002uyt
STRUCTURE OF L-RHAMNULOSE KINASE IN COMPLEX WITH ADP AND BETA-L-RHAMNULOSE.
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| 2uyt, resolution 1.55Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | ADP, LRH | ||||||||||||
| Activity: | Rhamnulokinase, with EC number 2.7.1.5 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
2UYT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures., Grueninger D, Schulz GE, FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582
Page seeded by OCA on Mon Mar 31 05:06:25 2008
