2aao
From Proteopedia
(New page: 200px<br /><applet load="2aao" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aao, resolution 2.000Å" /> '''Regulatory apparatu...) |
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| - | [[Image:2aao.gif|left|200px]]<br /><applet load="2aao" size=" | + | [[Image:2aao.gif|left|200px]]<br /><applet load="2aao" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2aao, resolution 2.000Å" /> | caption="2aao, resolution 2.000Å" /> | ||
'''Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana'''<br /> | '''Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calcium-dependent protein kinases (CDPKs) are a class of calcium-binding | + | Calcium-dependent protein kinases (CDPKs) are a class of calcium-binding sensory proteins that are found in plants and certain protozoa, including the causative agent of malaria, Plasmodium falciparum. CDPKs have diverse regulatory functions, including involvement in the triggering of the lytic cycle of malarial infection. CDPKs contain an autoinhibitory junction (J) region whose calcium-dependent interaction with the tethered regulatory calmodulin-like domain (CaM-LD) activates the catalytic kinase domain. We report here the X-ray crystal structure of the J-CaM-LD region of CDPK from Arabidopsis thaliana (AtCPK1), determined to 2.0 A resolution using multiple-wavelength anomalous dispersion (MAD). The structure reveals a symmetric dimer of calcium-bound J-CaM-LD with domain-swap interactions, in which the J region of one protomer interacts extensively with the carboxy-terminal EF-hand domain (C-lobe) of the partner protomer. However, as the J-CaM-LD is monomeric in solution, the activated monomer was modelled to account for the intra-molecular recognition of the two domains. While the J-CaM-LD segment mimics certain aspects of target motif recognition by CaM other features are specific to CDPKs, in particular the combination of the strong interaction between the N and C-lobes of the CaM-LD and the exclusive use of only the C-lobe in the recognition of the covalently tethered target region. Combined with our previous observations showing that there is likely to be strong interactions between this tethered J region and the CaM-LD even at basal Ca(2+) concentrations, the new structural data indicate that the response to calcium of CDPKs is clearly unique among the CaM family. |
==About this Structure== | ==About this Structure== | ||
| - | 2AAO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2AAO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] 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=2AAO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chandran, V.]] | [[Category: Chandran, V.]] | ||
| - | [[Category: Chazin, W | + | [[Category: Chazin, W J.]] |
[[Category: Christodoulou, J.]] | [[Category: Christodoulou, J.]] | ||
| - | [[Category: Dobson, C | + | [[Category: Dobson, C M.]] |
| - | [[Category: Harper, J | + | [[Category: Harper, J F.]] |
[[Category: Lindorff-Larsen, K.]] | [[Category: Lindorff-Larsen, K.]] | ||
| - | [[Category: Luisi, B | + | [[Category: Luisi, B F.]] |
| - | [[Category: Stollar, E | + | [[Category: Stollar, E J.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
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[[Category: ef hand]] | [[Category: ef hand]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:35 2008'' |
Revision as of 14:25, 21 February 2008
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Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana
Overview
Calcium-dependent protein kinases (CDPKs) are a class of calcium-binding sensory proteins that are found in plants and certain protozoa, including the causative agent of malaria, Plasmodium falciparum. CDPKs have diverse regulatory functions, including involvement in the triggering of the lytic cycle of malarial infection. CDPKs contain an autoinhibitory junction (J) region whose calcium-dependent interaction with the tethered regulatory calmodulin-like domain (CaM-LD) activates the catalytic kinase domain. We report here the X-ray crystal structure of the J-CaM-LD region of CDPK from Arabidopsis thaliana (AtCPK1), determined to 2.0 A resolution using multiple-wavelength anomalous dispersion (MAD). The structure reveals a symmetric dimer of calcium-bound J-CaM-LD with domain-swap interactions, in which the J region of one protomer interacts extensively with the carboxy-terminal EF-hand domain (C-lobe) of the partner protomer. However, as the J-CaM-LD is monomeric in solution, the activated monomer was modelled to account for the intra-molecular recognition of the two domains. While the J-CaM-LD segment mimics certain aspects of target motif recognition by CaM other features are specific to CDPKs, in particular the combination of the strong interaction between the N and C-lobes of the CaM-LD and the exclusive use of only the C-lobe in the recognition of the covalently tethered target region. Combined with our previous observations showing that there is likely to be strong interactions between this tethered J region and the CaM-LD even at basal Ca(2+) concentrations, the new structural data indicate that the response to calcium of CDPKs is clearly unique among the CaM family.
About this Structure
2AAO is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition., Chandran V, Stollar EJ, Lindorff-Larsen K, Harper JF, Chazin WJ, Dobson CM, Luisi BF, Christodoulou J, J Mol Biol. 2006 Mar 24;357(2):400-10. Epub 2005 Dec 20. PMID:16430916
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