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The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thalianaThe crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedArabidopsis 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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