2zfd

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(New page: 200px<br /><applet load="2zfd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2zfd, resolution 1.20&Aring;" /> '''The crystal structur...)
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Revision as of 17:01, 21 February 2008


2zfd, resolution 1.20Å

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The crystal structure of plant specific calcium binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14

Overview

Calcium signals mediate a multitude of plant responses to external stimuli. Calcineurin B-like (CBL) proteins and their target kinases, CBL-interacting protein kinases (CIPKs), represent important relays in plant calcium signaling. CBL interacts with CIPK through a conserved motif (NAF/FISL motif) within the C-terminal regulatory domain. To better understand the functional role of the CBL-CIPK system, we determined the crystal structure of AtCBL2 in complex with the regulatory domain of AtCIPK14 at 1.2 A resolution. The NAF/FISL motif is inserted into a hydrophobic crevice within AtCBL2, accompanied by a large displacement of the helices and loop on the opposite side of the NAF/FISL motif from the C-terminal region, which shields the hydrophobic crevice in free form. Ca(2+) are coordinated within four EF hands in AtCBL2 in bound form. This calcium coordination pattern differs from that in the structure of the SOS3-SOS2 complex previously reported. Structural comparison of the two structures shows that the recognition of CBL by CIPK is performed in a similar manner, but inherent interactions confer binding affinity and specificity.

About this Structure

2ZFD is a Protein complex structure of sequences from Arabidopsis thaliana with and as ligands. Full crystallographic information is available from OCA.

Reference

The Crystal Structure of Plant-Specific Calcium-Binding Protein AtCBL2 in Complex with the Regulatory Domain of AtCIPK14., Akaboshi M, Hashimoto H, Ishida H, Saijo S, Koizumi N, Sato M, Shimizu T, J Mol Biol. 2008 Jan 11;. PMID:18237745

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