Abstract
The crystal structure of calcium-bound unmyristoylated bovine neurocalcin from Escherichia coli has been determined at 2.4 Å resolution. The three-dimensional structure reveals a highly compact structure consisting of: (i) two pairs of calcium-binding EF-hands (EF1-EF2 and EF3-EF4); (ii) a calcium ion bound at EF2, EF3 and EF4 sites; and (iii) an EF1-hand that is disabled from calcium-binding due to a Cys-Pro sequence in the Ca 2+ -binding loop. The crystal structure of neurocalcin resembles photoreceptor recoverin in overall topology, however its EF2- and EF4-hands differ. Recently, neurocalcin in the calcium-bound state has been shown to stimulate mammalian rod outer segment membrane guanylate cyclase. A possible site for cyclase activity based on the three-dimensional structure is discussed.
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Acknowledgements
We thank I. Weber for comments on the manuscript. This work was funded in part by Markey's foundation (S.V.-K.) and Kimmel Cancer Center (V.D.K).
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Vijay-Kumar, S., Kumar, V. Crystal structure of recombinant bovine neurocalcin. Nat Struct Mol Biol 6, 80–88 (1999). https://doi.org/10.1038/4956
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DOI: https://doi.org/10.1038/4956
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