2uyt
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The enzyme L-rhamnulose kinase from Escherichia coli participates in the | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Grueninger, D.]] | [[Category: Grueninger, D.]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: LRH]] | [[Category: LRH]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:51:39 2008'' |
Revision as of 16:51, 21 February 2008
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STRUCTURE OF L-RHAMNULOSE KINASE IN COMPLEX WITH ADP AND BETA-L-RHAMNULOSE.
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 with and as ligands. Active as Rhamnulokinase, with EC number 2.7.1.5 Known structural/functional Site: . 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
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