PDBsum entry 1deg

Calcium-binding protein

PDB id

1deg

Contents

			Protein chain

					142 a.a.* *

			Metals

					_CA ×4

* Residue conservation analysis

* C-alpha coords only

PDB id:

1deg

Links

Name:

Calcium-binding protein

Title:

The linker of des-glu84 calmodulin is bent as seen in the crystal structure

Structure:

Calmodulin. Chain: a. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain.

Resolution:

2.90Å

R-factor:

0.230

Authors:

S.Raghunathan,R.Chandross,B.P.Cheng,A.Persechini,S.E.Sobottk, R.H.Kretsinger

Key ref:

S.Raghunathan et al. (1993). The linker of des-Glu84-calmodulin is bent. Proc Natl Acad Sci U S A, 90, 6869-6873. PubMed id: 8341712 DOI: 10.1073/pnas.90.14.6869

Date:

07-Jun-93

Release date:

31-May-94

	Headers

	References

Protein chain

P62157 (CALM_BOVIN) - Calmodulin from Bos taurus

Seq: Struc:					149 a.a. 142 a.a.*

Key:

Secondary structure

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

Key reference

DOI no: 10.1073/pnas.90.14.6869	Proc Natl Acad Sci U S A 90:6869-6873 (1993)
PubMed id: 8341712

The linker of des-Glu84-calmodulin is bent.
S.Raghunathan, R.J.Chandross, B.P.Cheng, A.Persechini, S.E.Sobottka, R.H.Kretsinger.

ABSTRACT

The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17173306

L.Settimo, S.Donnini, A.H.Juffer, R.W.Woody, and O.Marin (2007).
Conformational changes upon calcium binding and phosphorylation in a synthetic fragment of calmodulin.

Biopolymers, 88, 373-385.

12557181

L.A.Faga, B.R.Sorensen, W.S.VanScyoc, and M.A.Shea (2003).
Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions.

Proteins, 50, 381-391.

9037719

A.R.Khan, K.A.Johnson, J.Braam, and M.N.James (1997).
Comparative modeling of the three-dimensional structure of the calmodulin-related TCH2 protein from Arabidopsis.

Proteins, 27, 144-153.

PDB code:

1avj

9195880

L.Tabernero, D.A.Taylor, R.J.Chandross, M.F.VanBerkum, A.R.Means, F.A.Quiocho, and J.S.Sack (1997).
The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding.

Structure, 5, 613-622.

PDB code:

1ahr

7851407

G.Travé, A.Pastore, M.Hyvönen, and M.Saraste (1995).
The C-terminal domain of alpha-spectrin is structurally related to calmodulin.

Eur J Biochem, 227, 35-42.

8020480

K.Y.Ling, M.E.Maley, R.R.Preston, Y.Saimi, and C.Kung (1994).
New non-lethal calmodulin mutations in Paramecium. A structural and functional bipartition hypothesis.

Eur J Biochem, 222, 433-439.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.