1jb1
From Proteopedia
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- | [[Image:1jb1.gif|left|200px]] | + | [[Image:1jb1.gif|left|200px]] |
- | + | ||
- | '''Lactobacillus casei HprK/P Bound to Phosphate''' | + | {{Structure |
+ | |PDB= 1jb1 |SIZE=350|CAPTION= <scene name='initialview01'>1jb1</scene>, resolution 2.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= PTSK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei]) | ||
+ | }} | ||
+ | |||
+ | '''Lactobacillus casei HprK/P Bound to Phosphate''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1JB1 is a [ | + | 1JB1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JB1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11483495 11483495] |
[[Category: Lactobacillus casei]] | [[Category: Lactobacillus casei]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein kinase]] | [[Category: protein kinase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:00:58 2008'' |
Revision as of 10:01, 20 March 2008
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, resolution 2.8Å | |||||||
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Ligands: | |||||||
Gene: | PTSK (Lactobacillus casei) | ||||||
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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