1jb1: Difference between revisions

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[[Image:1jb1.gif|left|200px]]
{{Seed}}
[[Image:1jb1.png|left|200px]]


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{{STRUCTURE_1jb1|  PDB=1jb1  |  SCENE=  }}  
{{STRUCTURE_1jb1|  PDB=1jb1  |  SCENE=  }}  


'''Lactobacillus casei HprK/P Bound to Phosphate'''
===Lactobacillus casei HprK/P Bound to Phosphate===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_11483495}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11483495}}


==About this Structure==
==About this Structure==
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[[Category: P-loop]]
[[Category: P-loop]]
[[Category: Protein kinase]]
[[Category: Protein kinase]]
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