Crystal Structure of Calcium Bound Domain VI of Calpain at 1.9A Resolution and its Role in Enzyme Assembly, Regulation, and Inhibitor Binding.

Lin,G., Chattopadhyay, D., Maki, M., Wang, K.K.W., Carson, M., Jin, L.,Yuen, P., Takano, E., Hatanaka, M., DeLucas, L.J. and Narayana, S.V.L (accepted by Nature Struc. Biol.)

In this very interesting structure solved by Narayana, we observe a protein with 5 EF-hands. The protein has 2 normal pairs of EF-hands for calcium binding, and the 5th is involved structurally in dimer formation.

Dimer Structure (stereo)
Each monomer is a different color ribbon. The silver balls are the calciums.

OMITMAP around a Calcium-binding loop (stereo).
The map is magenta cagework, with color-coded atoms shown as balls-&-sticks. All atoms within 7 angstroms of the central calcium were omitted from the calculation. This gives an idea of the quality of the structure.

Difference map and Inhibitor (stereo).
The inhibitor binds in a hydrophobic pocket formed from two helices, much like what is observed with Calmodulin.