PDBsum entry 1prw

Metal binding protein

PDB id: 1prw

Contents

Protein chain

149 a.a. *

Metals

_CA ×4

Waters ×172

* Residue conservation analysis

PDB id:

1prw

Name:

Metal binding protein

Title:

Crystal structure of bovine brain ca++ calmodulin in a compact form

Structure:

Calmodulin. Chain: a

Source:

Bos taurus. Cattle. Organism_taxid: 9913

Resolution:

1.70Å R-factor: 0.186 R-free: 0.230

Authors:

J.L.Fallon,F.A.Quiocho

Key ref:

J.L.Fallon and F.A.Quiocho (2003). A closed compact structure of native Ca(2+)-calmodulin. Structure, 11, 1303-1307. PubMed id: 14527397 DOI: 10.1016/j.str.2003.09.004

Date:

20-Jun-03 Release date: 10-Oct-03

Protein chain

P62157  (CALM_BOVIN) -  Calmodulin from Bos taurus

Seq: 149 a.a.

Struc: 148 a.a.*

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

DOI no: 10.1016/j.str.2003.09.004

Structure 11:1303-1307 (2003)

PubMed id: 14527397

A closed compact structure of native Ca(2+)-calmodulin.

J.L.Fallon, F.A.Quiocho.

ABSTRACT

Calmodulin has been a subject of intense scrutiny since its discovery because of its unusual properties in regulating the functions of about 100 diverse target enzymes and structural proteins. The original and to date only crystal conformation of native eukaryotic Ca(2+)-calmodulin (Ca(2+)-CaM) is a very extended molecule with two widely separated globular domains linked by an exposed long helix. Here we report the 1.7 A X-ray structure of a new native Ca(2+)-CaM that is in a compact ellipsoidal conformation and shows a sharp bend in the linker helix and a more contracted N-terminal domain. This conformation may offer advantages for recognition of kinase-type calmodulin targets or small organic molecule drugs.

Selected figure(s)

Figure 1.
Figure 1. Unbound Compact Structure of Native Ca^2+-CaM(A) Stereoview of the electron density (2Fo-Fc at 1 s level) for the N-domain of Ca^2+-CaM, showing the N-terminal acetoalanine (n-ACE) and residues 2, 3, and 4 as a ball and stick model. Carbon atoms are green, oxygens are red, and nitrogens are blue.(B) Stereoview of the ribbon diagram of Ca^2+-CaM showing interdomain contacts. The CaM backbone is purple, loops are brown, and calciums are blue spheres. The sidechains that make contact (including 16 hydrogen bonds (<3.4 Å) and 24 van der Waals interactions (<4 Å)) between domains are shown (atom colors as Figure 1A, with sulfur yellow). Helices are numbered from I-VIII.

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1303-1307) copyright 2003.

Figure was selected by an automated process.