PDBsum entry 1s6j

Transferase, plant protein

PDB id: 1s6j

Contents

Protein chain

87 a.a. *

Metals

_CA ×2

* Residue conservation analysis

PDB id:

1s6j

Name:

Transferase, plant protein

Title:

N-terminal region of the ca2+-saturated calcium regulatory domain (cld) from soybean calcium-dependent protein kinase-alpha (cdpk)

Structure:

Calcium-dependent protein kinase sk5. Chain: a. Fragment: n-terminal region of calmodulin-like domain (cld). Synonym: cdpk. Calcium-dependent protein kinase-alpha. Engineered: yes

Source:

Glycine max. Soybean. Organism_taxid: 3847. Gene: cdpk sk5. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: 13 residues from an n-terminal his-tag, and the n- terminal domain of the ca2+-regulatory region

NMR struc:

15 models

Authors:

A.M.Weljie,H.J.Vogel

Key ref:

A.M.Weljie et al. (2004). Solution structure and backbone dynamics of the N-terminal region of the calcium regulatory domain from soybean calcium-dependent protein kinase alpha. Biochemistry, 43, 15131-15140. PubMed id: 15568805 DOI: 10.1021/bi048751r

Date:

23-Jan-04 Release date: 21-Dec-04

Protein chain

P28583  (CDPK_SOYBN) -  Calcium-dependent protein kinase SK5 from Glycine max

Seq: 508 a.a.

Struc: 87 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1021/bi048751r

Biochemistry 43:15131-15140 (2004)

PubMed id: 15568805

Solution structure and backbone dynamics of the N-terminal region of the calcium regulatory domain from soybean calcium-dependent protein kinase alpha.

A.M.Weljie, S.M.Gagné, H.J.Vogel.

ABSTRACT

Ca(2+)-dependent protein kinases (CDPKs) are vital Ca(2+)-signaling proteins in plants and protists which have both a kinase domain and a self-contained calcium regulatory calmodulin-like domain (CLD). Despite being very similar to CaM (>40% identity) and sharing the same fold, recent biochemical and structural evidence suggests that the behavior of CLD is distinct from its namesake, calmodulin. In this study, NMR spectroscopy is employed to examine the structure and backbone dynamics of a 168 amino acid Ca(2+)-saturated construct of the CLD (NtH-CLD) in which almost the entire C-terminal domain is exchange broadened and not visible in the NMR spectra. Structural characterization of the N-terminal domain indicates that the first Ca(2+)-binding loop is significantly more open than in a recently reported structure of the CLD complexed with a putative intramolecular binding region (JD) in the CDPK. Backbone dynamics suggest that parts of the third helix exhibit unusually high mobility, and significant exchange, consistent with previous findings that this helix interacts with the C-terminal domain. Dynamics data also show that the "tether" region, consisting of the first 11 amino acids of CLD, is highly mobile and these residues exhibit distinctive beta-type secondary structure, which may help to position the JD and CLD. Finally, the unusual global dynamic behavior of the protein is rationalized on the basis of possible interdomain rearrangements and the highly variable environments of the C- and N-terminal domains.