1jb1
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(New page: 200px<br /><applet load="1jb1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jb1, resolution 2.8Å" /> '''Lactobacillus casei H...)
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Revision as of 15:56, 20 November 2007
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Lactobacillus casei HprK/P Bound to Phosphate
Overview
HPr kinase/phosphatase (HprK/P) is a key regulatory enzyme controlling, carbon metabolism in Gram- positive bacteria. It catalyses the, ATP-dependent phosphorylation of Ser46 in HPr, a protein of the, phosphotransferase system, and also its dephosphorylation. HprK/P is, unrelated to eukaryotic protein kinases, but contains the Walker motif A, characteristic of nucleotide-binding proteins. We report here the X-ray, structure of an active fragment of Lactobacillus casei HprK/P at 2.8 A, resolution, solved by the multiwavelength anomalous dispersion method on a, seleniated protein (PDB code 1jb1). The protein is a hexamer, with each, subunit containing an ATP-binding domain similar to nucleoside/nucleotide, kinases, and a putative HPr-binding domain unrelated to the, substrate-binding domains of other kinases. The Walker motif A forms a, typical P-loop which binds inorganic phosphate in the crystal. We modelled, ATP binding by comparison with adenylate kinase, and designed a tentative, model of the complex with HPr based on a docking simulation. The results, confirm that HprK/P represents a new family of protein kinases, first, identified in bacteria, but which may also have members in eukaryotes.
About this Structure
1JB1 is a Single protein structure of sequence from Lactobacillus casei with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain., Fieulaine S, Morera S, Poncet S, Monedero V, Gueguen-Chaignon V, Galinier A, Janin J, Deutscher J, Nessler S, EMBO J. 2001 Aug 1;20(15):3917-27. PMID:11483495
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