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PDBsum entry 4cln

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Calcium binding protein PDB id
4cln
Contents
Protein chain
148 a.a.
Metals
_CA ×4
Waters ×78

References listed in PDB file
Key reference
Title Structure of a recombinant calmodulin from drosophila melanogaster refined at 2.2-A resolution.
Authors D.A.Taylor, J.S.Sack, J.F.Maune, K.Beckingham, F.A.Quiocho.
Ref. J Biol Chem, 1991, 266, 21375-21380.
PubMed id 1939171
Abstract
The crystal structure of calmodulin (Mr 16,700, 148 residues) from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution. Starting with the structure of mammalian calmodulin, we produced an extensively refitted and refined model with a conventional crystallographic R value of 0.197 for the 5,239 reflections (F greater than or equal to 2 sigma (F)) within the 10.0-2.2-A resolution range. The model includes 1,164 protein atoms, 4 calcium ions, and 78 water molecules and has root mean square deviations from standard values of 0.018 A for bond lengths and 0.043 A for angle distances. The overall structure is similar to mammalian calmodulin, with a seven-turn central helix connecting the two calcium-binding domains. The "dumb-bell" shaped molecule contains seven alpha-helices and four "EF hand" calcium-binding sites. Although the amino acid sequences of mammalian and Drosophila calmodulins differ by only three conservative amino acid changes, the refined model reveals a number of significant differences between the two structures. Superimposition of the structures yields a root mean square deviation of 1.22 A for the 1,120 equivalent atoms. The calcium-binding domains have a root mean square deviation of 0.85 A for the 353 equivalent atoms. There are also differences in the amino terminus, the bend of the central alpha-helix, and the orientations of some of the side chains.
Secondary reference #1
Title Structure and sequence of the drosophila melanogaster calmodulin gene.
Authors V.L.Smith, K.E.Doyle, J.F.Maune, R.P.Munjaal, K.Beckingham.
Ref. J Mol Biol, 1987, 196, 471-485.
PubMed id 3119855
Abstract
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