PDBsum entry 1cff

Calmodulin

PDB id: 1cff

Contents

Protein chains

148 a.a. *

20 a.a. *

Metals

_CA ×4

* Residue conservation analysis

PDB id:

1cff

Name:

Calmodulin

Title:

Nmr solution structure of a complex of calmodulin with a binding peptide of the ca2+-pump

Structure:

Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Calcium pump. Chain: b. Fragment: cam-binding domain. Engineered: yes. Mutation: yes

Source:

Xenopus laevis. African clawed frog. Organism_taxid: 8355. Strain: 71. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Homo sapiens. Organism_taxid: 9606

NMR struc:

26 models

Authors:

B.Elshorst,M.Hennig,H.Foersterling,A.Diener,M.Maurer,P.Schulte, H.Schwalbe,J.Krebs,H.Schmid,T.Vorherr,E.Carafoli,C.Griesinger

Key ref:

B.Elshorst et al. (1999). NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry, 38, 12320-12332. PubMed id: 10493800 DOI: 10.1021/bi9908235

Date:

18-Mar-99 Release date: 24-Sep-99

Protein chain

P0DP33  (CALM1_XENLA) -  Calmodulin-1 from Xenopus laevis

Seq: 149 a.a.

Struc: 148 a.a.

Protein chain

P23634  (AT2B4_HUMAN) -  Plasma membrane calcium-transporting ATPase 4 from Homo sapiens

Seq: 1241 a.a.

Struc: 20 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chain B: E.C.7.2.2.10 - P-type Ca(2+) transporter.
• Reaction: Ca²⁺(in) + ATP + H2O = Ca²⁺(out) + ADP + phosphate + H⁺
• Cofactor: Mg(2+)

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

reference

DOI no: 10.1021/bi9908235

Biochemistry 38:12320-12332 (1999)

PubMed id: 10493800

NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.

B.Elshorst, M.Hennig, H.Försterling, A.Diener, M.Maurer, P.Schulte, H.Schwalbe, C.Griesinger, J.Krebs, H.Schmid, T.Vorherr, E.Carafoli.

ABSTRACT

The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the plasma membrane calcium pump, the peptide C20W, has been solved by heteronuclear three-dimensional nuclear magnetic resonance (NMR) spectroscopy. The structure calculation is based on a total of 1808 intramolecular NOEs and 49 intermolecular NOEs between the peptide C20W and calmodulin from heteronuclear-filtered NOESY spectra and a half-filtered experiment, respectively. Chemical shift differences between free Ca(2+)-saturated CaM and its complex with C20W as well as the structure calculation reveal that C20W binds solely to the C-terminal half of CaM. In addition, comparison of the methyl resonances of the nine assigned methionine residues of free Ca(2+)-saturated CaM with those of the CaM/C20W complex revealed a significant difference between the N-terminal and the C-terminal domain; i.e., resonances in the N-terminal domain of the complex were much more similar to those reported for free CaM in contrast to those in the C-terminal half which were significantly different not only from the resonances of free CaM but also from those reported for the CaM/M13 complex. As a consequence, the global structure of the CaM/C20W complex is unusual, i.e., different from other peptide calmodulin complexes, since we find no indication for a collapsed structure. The fine modulation in the peptide protein interface shows a number of differences to the CaM/M13 complex studied by Ikura et al. [Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Science 256, 632-638]. The unusual binding mode to only the C-terminal half of CaM is in agreement with the biochemical observation that the calcium pump can be activated by the C-terminal half of CaM alone [Guerini, D., Krebs, J., and Carafoli, E. (1984) J. Biol. Chem. 259, 15172-15177].