2ddm

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spinqualitylabelsall models 2ddm, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene at 2.1 A resolution

Overview

The pdxK and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal phosphate salvage pathway. Two pyridoxal, kinase structures have recently been published, including Escherichia coli, pyridoxal kinase 2 (ePL kinase 2) and sheep pyridoxal kinase, products of, the pdxY and pdxK genes, respectively. We now report the crystal structure, of E. coli pyridoxal kinase 1 (ePL kinase 1), encoded by a pdxK gene, and, an isoform of ePL kinase 2. The structures were determined in the, unliganded and binary complexes with either MgATP or pyridoxal to 2.1-, 2.6-, and 3.2-A resolutions, respectively. The active site of ePL kinase 1, does not show significant conformational change upon binding of either, pyridoxal or MgATP. Like sheep PL kinase, ePL kinase 1 exhibits a, sequential random mechanism. Unlike sheep pyridoxal kinase, ePL kinase 1, may not tolerate wide variation in the size and chemical nature of the 4', substituent on the substrate. This is the result of differences in a key, residue at position 59 on a loop (loop II) that partially forms the active, site. Residue 59, which is His in ePL kinase 1, interacts with the formyl, group at C-4' of pyridoxal and may also determine if residues from another, loop (loop I) can fill the active site in the absence of the substrate., Both loop I and loop II are suggested to play significant roles in the, functions of PL kinases.

About this Structure

2DDM is a Single protein structure of sequence from Escherichia coli with TRS as ligand. Active as Pyridoxal kinase, with EC number 2.7.1.35 Full crystallographic information is available from OCA.

Reference

Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases., Safo MK, Musayev FN, di Salvo ML, Hunt S, Claude JB, Schirch V, J Bacteriol. 2006 Jun;188(12):4542-52. PMID:16740960

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