1jb1

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{{STRUCTURE_1jb1| PDB=1jb1 | SCENE= }}
{{STRUCTURE_1jb1| PDB=1jb1 | SCENE= }}
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'''Lactobacillus casei HprK/P Bound to Phosphate'''
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===Lactobacillus casei HprK/P Bound to Phosphate===
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==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.
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==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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 19:56:45 2008''

Revision as of 16:56, 1 July 2008

Image:1jb1.png

Template:STRUCTURE 1jb1

Lactobacillus casei HprK/P Bound to Phosphate

Template:ABSTRACT PUBMED 11483495

About this Structure

1JB1 is a Single protein structure of sequence from Lactobacillus casei. 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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