1s6i
From Proteopedia
| |||||||
| Ligands: | |||||||
| Gene: | CDPK SK5 (Glycine max) | ||||||
| Related: | 1S6J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ca2+-regulatory region (CLD) from soybean calcium-dependent protein kinase-alpha (CDPK) in the presence of Ca2+ and the junction domain (JD)
Overview
Calcium-dependent protein kinases (CDPKs) are an extensive class of multidomain Ca(2+)-regulated enzymes from plants and protozoa. In vivo the so-called calmodulin-like domain (CLD) of CDPK binds intramolecularly to the junction domain (JD), which exhibits both kinase-inhibitory and CLD binding properties. Here we report the high resolution solution structure of the calcium-regulatory region from soybean CDPK-alpha determined in the presence of a peptide encompassing the JD. The structure of both lobes of CLD resembles that of related helix-loop-helix Ca(2+)-binding proteins. NMR chemical shift mapping studies demonstrate that the JD induces significant structural changes in isolated Ca(2+)-CLD, particularly the C-terminal domain, although a stable complex is not formed. A CLD solution structure calculated on the basis of NMR data and long range fluorescence resonance energy transfer distances reveals an activated state with both lobes positioned side by side, similar to calcineurin B rather than calmodulin, highlighting the possible pitfall of assigning function purely from sequence information.
About this Structure
1S6I is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-alpha., Weljie AM, Vogel HJ, J Biol Chem. 2004 Aug 20;279(34):35494-502. Epub 2004 May 20. PMID:15155727
Page seeded by OCA on Sun Mar 30 23:38:07 2008
