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Proteins. 2009 Aug 1;76(2):477-83. doi: 10.1002/prot.22362.

X-ray structure of Danio rerio secretagogin: A hexa-EF-hand calcium sensor.

Author information

1
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, 53706-1544, USA.

Abstract

Many essential physiological processes are regulated by the modulation of calcium concentration in the cell. The EF-hand proteins represent a superfamily of calcium-binding proteins involved in calcium signaling and homeostasis. Secretagogin is a hexa-EF-hand protein that is highly expressed in pancreatic islet of Langerhans and neuroendocrine cells and may play a role in the trafficking of secretory granules. We present the X-ray structure of Danio rerio secretagogin, which is 73% identical to human secretagogin, in calcium-free form at 2.1-A resolution. Secretagogin consists of the three globular domains each of which contains a pair of EF-hand motifs. The domains are arranged into a V-shaped molecule with a distinct groove formed at the interface of the domains. Comparison of the secretagogin structure with the solution structure of calcium-loaded calbindin D(28K) revealed a striking difference in the spatial arrangement of their domains, which involves approximately 180 degrees rotation of the first globular domain with respect to the module formed by the remaining domains.

PMID:
19241471
PMCID:
PMC2742686
DOI:
10.1002/prot.22362
[Indexed for MEDLINE]
Free PMC Article

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