PDBsum entry 4bw7

Metal binding protein

PDB id

4bw7

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Contents

			Protein chains

					137 a.a.


					146 a.a.

			Metals

					_SR ×9

			Waters ×231

PDB id:

4bw7

Links

Name:

Metal binding protein

Title:

Calmodulin in complex with strontium

Structure:

Calmodulin. Chain: a, c. Synonym: cam. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta.

Resolution:

1.81Å

R-factor:

0.208

R-free:

0.251

Authors:

P.Kursula

Key ref:

P.Kursula (2014). Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix. Acta Crystallogr D Biol Crystallogr, 70, 24-30. PubMed id: 24419375 DOI: 10.1107/S1399004713024437

Date:

30-Jun-13

Release date:

15-Jan-14

PROCHECK

	Headers

	References

Protein chain

P0DP23 (CALM1_HUMAN) - Calmodulin-1 from Homo sapiens

Seq: Struc:					149 a.a. 137 a.a.

Protein chain

P0DP23 (CALM1_HUMAN) - Calmodulin-1 from Homo sapiens

Seq: Struc:					149 a.a. 146 a.a.

Key:

PfamA domain

Secondary structure

DOI no: 10.1107/S1399004713024437	Acta Crystallogr D Biol Crystallogr 70:24-30 (2014)
PubMed id: 24419375

Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix.
P.Kursula.

ABSTRACT

Calmodulin is one of the most well characterized proteins and a widely used model system for calcium binding and large-scale protein conformational changes. Its long central helix is usually cut in half when a target peptide is bound. Here, two new crystal structures of calmodulin are presented, in which conformations possibly representing the first steps of calmodulin conformational collapse have been trapped. The central helix in the two structures is bent in the middle, causing a significant movement of the N- and C-terminal lobes with respect to one another. In both of the bent structures, a nearby polar side chain is inserted into the helical groove, disrupting backbone hydrogen bonding. The structures give an insight into the details of the factors that may be involved in the distortion of the central helix upon ligand peptide binding.