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| | {{STRUCTURE_2aao| PDB=2aao | SCENE= }} | | {{STRUCTURE_2aao| PDB=2aao | SCENE= }} |
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| - | '''Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana'''
| + | ===Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16430916}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16430916 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16430916}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Calmodulin-like domain]] | | [[Category: Calmodulin-like domain]] |
| | [[Category: Ef hand]] | | [[Category: Ef hand]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:49:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:30:35 2008'' |
Revision as of 10:30, 27 July 2008
Template:STRUCTURE 2aao
Regulatory apparatus of Calcium Dependent protein kinase from Arabidopsis thaliana
Template:ABSTRACT PUBMED 16430916
About this Structure
2AAO is a Single protein structure of sequence from Arabidopsis thaliana. 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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