2cgj

From Proteopedia

Revision as of 15:02, 30 October 2007

CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE AND ADP.

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

2CGJ is a [Single protein] structure of sequence from [Escherichia coli] with LFR and ADP as [ligands]. Active as [Rhamnulokinase], with EC number [2.7.1.5]. Structure known Active Site: AC1. 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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