2BCX

Crystal structure of calmodulin in complex with a ryanodine receptor peptide

Summary for 2BCX

• Entry DOI: 10.2210/pdb2bcx/pdb
• Descriptor: Calmodulin, Ryanodine receptor 1, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: ef-hand, type-2 turn, calcium binding protein
• Biological source: Gallus gallus (chicken); More
• Cellular location: Sarcoplasmic reticulum membrane ; Multi-pass membrane protein : P11716
• Total number of polymer chains: 2
• Total formula weight: 20508.10

Authors

Maximciuc, A.A.,Shamoo, Y.,MacKenzie, K.R. (deposition date: 2005-10-19, release date: 2006-10-31, Last modification date: 2024-02-14)

Primary citation

Maximciuc, A.A.,Putkey, J.A.,Shamoo, Y.,Mackenzie, K.R.
Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode.
Structure, 14:1547-1556, 2006

PubMed Abstract: Calmodulin regulates ryanodine receptor-mediated Ca(2+) release through a conserved binding site. The crystal structure of Ca(2+)-calmodulin bound to this conserved site reveals that calmodulin recognizes two hydrophobic anchor residues at a novel "1-17" spacing that brings the calmodulin lobes close together but prevents them from contacting one another. NMR residual dipolar couplings demonstrate that the detailed structure of each lobe is preserved in solution but also show that the lobes experience domain motions within the complex. FRET measurements confirm the close approach of the lobes in binding the 1-17 target and show that calmodulin binds with one lobe to a peptide lacking the second anchor. We suggest that calmodulin regulates the Ca(2+) channel by switching between the contiguous binding mode seen in our crystal structure and a state where one lobe of calmodulin contacts the conserved binding site while the other interacts with a noncontiguous site on the channel.

PubMed: 17027503
DOI: 10.1016/j.str.2006.08.011

Experimental method

X-RAY DIFFRACTION (2 Å)