1dmo
From Proteopedia
| |||||||
| Gene: | XENOPUS LAEVIS (Xenopus laevis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CALMODULIN, NMR, 30 STRUCTURES
Overview
The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.
About this Structure
1DMO is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Calcium-induced conformational transition revealed by the solution structure of apo calmodulin., Zhang M, Tanaka T, Ikura M, Nat Struct Biol. 1995 Sep;2(9):758-67. PMID:7552747
Page seeded by OCA on Sun Mar 30 19:44:48 2008
