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1jb1
From Proteopedia
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|PDB= 1jb1 |SIZE=350|CAPTION= <scene name='initialview01'>1jb1</scene>, resolution 2.8Å | |PDB= 1jb1 |SIZE=350|CAPTION= <scene name='initialview01'>1jb1</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PTSK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei]) | |GENE= PTSK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jb1 OCA], [http://www.ebi.ac.uk/pdbsum/1jb1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jb1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Nessler, S.]] | [[Category: Nessler, S.]] | ||
[[Category: Poncet, S.]] | [[Category: Poncet, S.]] | ||
| - | [[Category: PO4]] | ||
[[Category: catabolite repression]] | [[Category: catabolite repression]] | ||
[[Category: hexamer]] | [[Category: hexamer]] | ||
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[[Category: protein kinase]] | [[Category: protein kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:03 2008'' |
Revision as of 18:31, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PTSK (Lactobacillus casei) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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