2UYT: Structure Of L-Rhamnulose Kinase In Complex With Adp And Beta-L-Rhamnulose

Citation:
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.
PDB ID: 2UYTDownload
MMDB ID: 54349
PDB Deposition Date: 2007/4/13
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Similar Structures:
Biological Unit for 2UYT: monomeric; determined by author and by software (PQS)
Molecular Components in 2UYT
Label Count Molecule
Protein (1 molecule)
1
Rhamnulokinase(Gene symbol: rhaB)
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

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