1JWD

Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.

Summary for 1JWD

• Entry DOI: 10.2210/pdb1jwd/pdb
• Related: 1A03 1CNP 2CNP
• NMR Information: BMRB: 4430
• Descriptor: Calcyclin (1 entity in total)
• Functional Keywords: ca(2+)-binding protein, s100 protein, ef-hand, s100a6, metal binding protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Nucleus envelope (By similarity): P30801
• Total number of polymer chains: 2
• Total formula weight: 20335.46

Authors

Maler, L.,Sastry, M.,Chazin, W.J. (deposition date: 2001-09-04, release date: 2002-03-27, Last modification date: 2024-05-22)

Primary citation

Maler, L.,Sastry, M.,Chazin, W.J.
A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin
J.Mol.Biol., 317:279-290, 2002

PubMed Abstract: Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.

PubMed: 11902843
DOI: 10.1006/jmbi.2002.5421

Experimental method

SOLUTION NMR