1kkl

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[[Image:1kkl.gif|left|200px]]<br /><applet load="1kkl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kkl.gif|left|200px]]
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caption="1kkl, resolution 2.80&Aring;" />
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'''L.casei HprK/P in complex with B.subtilis HPr'''<br />
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{{Structure
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|PDB= 1kkl |SIZE=350|CAPTION= <scene name='initialview01'>1kkl</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE= PTSK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei]), PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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}}
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'''L.casei HprK/P in complex with B.subtilis HPr'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KKL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKL OCA].
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1KKL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKL OCA].
==Reference==
==Reference==
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X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr., Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12359875 12359875]
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X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr., Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12359875 12359875]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Lactobacillus casei]]
[[Category: Lactobacillus casei]]
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[[Category: protein/protein interaction]]
[[Category: protein/protein interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:42 2008''

Revision as of 10:18, 20 March 2008


PDB ID 1kkl

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Gene: PTSK (Lactobacillus casei), PTSH (Bacillus subtilis)
Coordinates: save as pdb, mmCIF, xml



L.casei HprK/P in complex with B.subtilis HPr


Overview

HPr kinase/phosphorylase (HprK/P) controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by Gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. We present here two crystal structures of a complex of the catalytic domain of Lactobacillus casei HprK/P with Bacillus subtilis HPr, both at 2.8-A resolution. One of the structures was obtained in the presence of excess pyrophosphate, reversing the phosphorolysis reaction and contains serine-phosphorylated HPr. The complex has six HPr molecules bound to the hexameric kinase. Two adjacent enzyme subunits are in contact with each HPr molecule, one through its active site and the other through its C-terminal helix. In the complex with serine-phosphorylated HPr, a phosphate ion is in a position to perform a nucleophilic attack on the phosphoserine. Although the mechanism of the phosphorylation reaction resembles that of eukaryotic protein kinases, the dephosphorylation by inorganic phosphate is unique to the HprK/P family of kinases. This study provides the structure of a protein kinase in complex with its protein substrate, giving insights into the chemistry of the phospho-transfer reactions in both directions.

About this Structure

1KKL is a Protein complex structure of sequences from Bacillus subtilis and Lactobacillus casei. Full crystallographic information is available from OCA.

Reference

X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr., Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. PMID:12359875

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