1UHN
The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana
Summary for 1UHN
| Entry DOI | 10.2210/pdb1uhn/pdb |
| Related | 1AUI |
| Descriptor | calcineurin B-like protein 2, CALCIUM ION (3 entities in total) |
| Functional Keywords | calcium binding protein, metal binding protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 21988.05 |
| Authors | Nagae, M.,Nozawa, A.,Koizumi, N.,Sano, H.,Hashimoto, H.,Sato, M.,Shimizu, T. (deposition date: 2003-07-07, release date: 2003-11-04, Last modification date: 2023-12-27) |
| Primary citation | Nagae, M.,Nozawa, A.,Koizumi, N.,Sano, H.,Hashimoto, H.,Sato, M.,Shimizu, T. The Crystal Structure of the Novel Calcium-binding Protein AtCBL2 from Arabidopsis thaliana J.Biol.Chem., 278:42240-42246, 2003 Cited by PubMed Abstract: 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. PubMed: 12871972DOI: 10.1074/jbc.M303630200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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