2i5b
From Proteopedia
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The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution
Overview
Pyridoxal kinase catalyses the phosphorylation of pyridoxal, pyridoxine, and pyridoxamine to their 5' phosphates and plays an important role in the, pyridoxal 5' phosphate salvage pathway. The crystal structure of a dimeric, pyridoxal kinase from Bacillus subtilis has been solved in complex with, ADP to 2.8 A resolution. Analysis of the structure suggests that binding, of the nucleotide induces the ordering of two loops, which operate, independently to close a flap on the active site. Comparisons with other, ribokinase superfamily members reveal that B. subtilis pyridoxal kinase is, more closely related in both sequence and structure to the family of HMPP, kinases than to other pyridoxal kinases, suggesting that this structure, represents the first for a novel family of "HMPP kinase-like" pyridoxal, kinases. Moreover this further suggests that this enzyme activity has, evolved independently on multiple occasions from within the ribokinase, superfamily.
About this Structure
2I5B is a Single protein structure of sequence from Bacillus subtilis with ADP as ligand. Active as Phosphomethylpyrimidine kinase, with EC number 2.7.4.7 Full crystallographic information is available from OCA.
Reference
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution., Newman JA, Das SK, Sedelnikova SE, Rice DW, J Mol Biol. 2006 Oct 20;363(2):520-30. Epub 2006 Aug 12. PMID:16978644
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