1uhn
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(New page: 200px<br /><applet load="1uhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uhn, resolution 2.1Å" /> '''The crystal structure...)
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Revision as of 02:00, 21 November 2007
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The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana
Overview
Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a, recently identified family of calcineurin B-like calcium-binding proteins, in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1, A resolution. The protein forms a compact alpha-helical structure with two, pairs of EF-hand motifs. The structure is similar in overall folding, topology to the structures of calcineurin B and neuronal calcium sensor 1, but differs significantly in local conformation. The two calcium ions are, coordinated in the first and fourth EF-hand motifs, whereas the second and, third EF-hand motifs are maintained in the open form by internal hydrogen, bonding without coordination of calcium ions. Both a possible site and a, possible mechanism for the target binding to AtCBL2 are discussed based on, the three-dimensional structure.
About this Structure
1UHN is a Single protein structure of sequence from Arabidopsis thaliana with CA as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana., Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T, J Biol Chem. 2003 Oct 24;278(43):42240-6. Epub 2003 Jul 19. PMID:12871972
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