1JB1

Lactobacillus casei HprK/P Bound to Phosphate

Summary for 1JB1

• Entry DOI: 10.2210/pdb1jb1/pdb
• Descriptor: HPRK PROTEIN, PHOSPHATE ION (3 entities in total)
• Functional Keywords: catabolite repression, hpr phosphorylation, lactobacillus casei, p-loop, protein kinase, hexamer, transferase-hydrolase complex, transferase/hydrolase
• Biological source: Lactobacillus casei
• Total number of polymer chains: 1
• Total formula weight: 23055.99

Authors

Fieulaine, S.,Morera, S.,Poncet, S.,Monedero, V.,Gueguen-Chaignon, V.,Galinier, A.,Janin, J.,Deutscher, J.,Nessler, S. (deposition date: 2001-06-01, release date: 2001-08-08, Last modification date: 2024-11-06)

Primary citation

Fieulaine, S.,Morera, S.,Poncet, S.,Monedero, V.,Gueguen-Chaignon, V.,Galinier, A.,Janin, J.,Deutscher, J.,Nessler, S.
X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain.
EMBO J., 20:3917-3927, 2001

PubMed Abstract: 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.

PubMed: 11483495
DOI: 10.1093/emboj/20.15.3917

Experimental method

X-RAY DIFFRACTION (2.8 Å)