2pvr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2pvr.gif|left|200px]] | [[Image:2pvr.gif|left|200px]] | ||
'''Crystal structure of the catalytic subunit of protein kinase CK2 (C-terminal deletion mutant 1-335) in complex with two sulfate ions''' | {{Structure | ||
|PDB= 2pvr |SIZE=350|CAPTION= <scene name='initialview01'>2pvr</scene>, resolution 1.605Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | |||
|GENE= CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of the catalytic subunit of protein kinase CK2 (C-terminal deletion mutant 1-335) in complex with two sulfate ions''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2PVR is a [ | 2PVR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVR OCA]. | ||
==Reference== | ==Reference== | ||
Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:[http:// | Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17524418 17524418] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
| Line 20: | Line 29: | ||
[[Category: ANP]] | [[Category: ANP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: cmgc | [[Category: cmgc kinase]] | ||
[[Category: eukaryotic protein kinase fold]] | [[Category: eukaryotic protein kinase fold]] | ||
''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 18:17:59 2008'' | ||
Revision as of 19:18, 20 March 2008
| |||||||
| , resolution 1.605Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CSNK2A1, CK2A1 (Homo sapiens) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the catalytic subunit of protein kinase CK2 (C-terminal deletion mutant 1-335) in complex with two sulfate ions
OverviewOverview
CK2alpha is the catalytic subunit of protein kinase CK2 and a member of the CMGC family of eukaryotic protein kinases like the cyclin-dependent kinases, the MAP kinases and glycogen-synthase kinase 3. We present here a 1.6 A resolution crystal structure of a fully active C-terminal deletion mutant of human CK2alpha liganded by two sulfate ions, and we compare this structure systematically with representative structures of related CMGC kinases. The two sulfate anions occupy binding pockets at the activation segment and provide the structural basis of the acidic consensus sequence S/T-D/E-X-D/E that governs substrate recognition by CK2. The anion binding sites are conserved among those CMGC kinases. In most cases they are neutralized by phosphorylation of a neighbouring threonine or tyrosine side-chain, which triggers conformational changes for regulatory purposes. CK2alpha, however, lacks both phosphorylation sites at the activation segment and structural plasticity. Here the anion binding sites are functionally changed from regulation to substrate recognition. These findings underline the exceptional role of CK2alpha as a constitutively active enzyme within a family of strictly controlled protein kinases.
About this StructureAbout this Structure
2PVR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:17524418
Page seeded by OCA on Thu Mar 20 18:17:59 2008