1S6I
Ca2+-regulatory region (CLD) from soybean calcium-dependent protein kinase-alpha (CDPK) in the presence of Ca2+ and the junction domain (JD)
Summary for 1S6I
| Entry DOI | 10.2210/pdb1s6i/pdb |
| Related | 1S6J |
| NMR Information | BMRB: 6104 |
| Descriptor | Calcium-dependent protein kinase SK5, CALCIUM ION (2 entities in total) |
| Functional Keywords | ef-hand; helix-loop-helix; calcium-binding; calmodulin superfamily, transferase, plant protein |
| Biological source | Glycine max (soybean) |
| Total number of polymer chains | 1 |
| Total formula weight | 21420.96 |
| Authors | Weljie, A.M.,Vogel, H.J. (deposition date: 2004-01-23, release date: 2004-06-15, Last modification date: 2024-05-22) |
| Primary citation | Weljie, A.M.,Vogel, H.J. Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-alpha J.Biol.Chem., 279:35494-35502, 2004 Cited by PubMed Abstract: 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. PubMed: 15155727DOI: 10.1074/jbc.M311520200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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