2cgl
From Proteopedia
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CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE, ADP AND A MODELED ATP GAMMA PHOSPHATE.
Overview
Bacterial L-rhamnulose kinase participates in the degradation of, L-rhamnose, which is ubiquitous and particularly abundant in some plants., The enzyme catalyzes the transfer of the gamma-phosphate group from ATP to, the 1-hydroxyl group of L-rhamnulose. We determined the crystal structures, of the substrate-free kinase and of a complex between the enzyme, ADP and, L-fructose, which besides rhamnulose is also processed. According to its, chainfold, the kinase belongs to the hexokinase-hsp70-actin superfamily., The closest structurally known homologue is glycerol kinase. The reported, structures reveal a large conformational change on substrate binding as, well as the key residues involved in catalysis. The substrates ADP and, beta-L-fructose are in an ideal position to define a direct ... [(full description)]
About this Structure
2CGL is a [Single protein] structure of sequence from [Escherichia coli] with LFR and ADP as [ligands]. Active as [[1]], with EC number [2.7.1.5]. Full crystallographic information is available from [OCA].
Reference
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:16674975
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