4BW8

Calmodulin with small bend in central helix

Summary for 4BW8

• Entry DOI: 10.2210/pdb4bw8/pdb
• Related: 4BW7
• Descriptor: CALMODULIN, CALCIUM ION (3 entities in total)
• Functional Keywords: metal binding protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 34025.71

Authors

Kursula, P. (deposition date: 2013-06-30, release date: 2014-01-15, Last modification date: 2023-12-20)

Primary citation

Kursula, P.
Crystallographic Snapshots of Initial Steps in the Collapse of the Calmodulin Central Helix
Acta Crystallogr.,Sect.D, 70:24-, 2014

PubMed 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.

PubMed: 24419375
DOI: 10.1107/S1399004713024437

Experimental method

X-RAY DIFFRACTION (1.8 Å)