PDBsum entry 1sw8

Calcium-binding protein

PDB id: 1sw8

Contents

Protein chain

79 a.a. *

Metals

_CA ×2

* Residue conservation analysis

PDB id:

1sw8

Name:

Calcium-binding protein

Title:

Solution structure of the n-terminal domain of human n60d calmodulin refined with paramagnetism based strategy

Structure:

Calmodulin. Chain: a. Fragment: n-terminal domain. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

I.Bertini,C.Del Bianco,I.Gelis,N.Katsaros,C.Luchinat,G.Parigi, M.Peana,A.Provenzani,M.A.Zoroddu,Structural Proteomics In Europe (Spine)

Key ref:

I.Bertini et al. (2004). Experimentally exploring the conformational space sampled by domain reorientation in calmodulin. Proc Natl Acad Sci U S A, 101, 6841-6846. PubMed id: 15100408 DOI: 10.1073/pnas.0308641101

Date:

30-Mar-04 Release date: 06-Apr-04

Protein chain

P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens

Seq: 149 a.a.

Struc: 79 a.a.*

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

DOI no: 10.1073/pnas.0308641101

Proc Natl Acad Sci U S A 101:6841-6846 (2004)

PubMed id: 15100408

Experimentally exploring the conformational space sampled by domain reorientation in calmodulin.

I.Bertini, C.Del Bianco, I.Gelis, N.Katsaros, C.Luchinat, G.Parigi, M.Peana, A.Provenzani, M.A.Zoroddu.

ABSTRACT

The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb(3+)- and Tm(3+)-substituted proteins. The observables are the pseudocontact shifts and residual dipolar couplings of the C-terminal domain when lanthanide substitution is at the N-terminal domain. Each set of observables provides independent information on the conformations experienced by the molecule. It is found that not all sterically allowed conformations are equally populated. Taking the N-terminal domain as the reference, the C-terminal domain preferentially resides in a region of space inscribed in a wide elliptical cone. The axis of the cone is tilted by approximately 30 degrees with respect to the direction of the N-terminal part of the interdomain helix, which is known to have a flexible central part in solution. The C-terminal domain also undergoes rotation about the axis defined by the C-terminal part of the interdomain helix. Neither the extended helix conformation initially observed in the solid state for free calcium calmodulin nor the closed conformation(s) adopted by calcium calmodulin either alone or in its adduct(s) with target peptide(s) is among the most preferred ones. These findings are unique, both in terms of structural information obtained on a biomolecule that samples multiple conformations and in terms of the approach developed to achieve the results. The same approach is in principle applicable to other multidomain proteins, as well as to multiple interaction modes between two macromolecular partners.

Selected figure(s)

Figure 1.
Fig. 1. Relative orientation of the N-terminal and C-terminal domains in CaM as early observed by x-ray in the absence of target peptides (A; extended conformation) and as observed in the presence of target peptides (B; closed conformation). Labels N4 and C1 indicate the fourth helix of the N-terminal domain and the first helix of the C-terminal domain, respectively.

Figure 5.
Fig. 5. Cone containing the three conformations of the C-terminal domain (only the first two helices are shown), which provide pcs and rdc with an average in good fit with the experimental data.

Figures were selected by an automated process.