2BE4

X-RAY STRUCTURE AN EF-HAND PROTEIN FROM DANIO RERIO Dr.36843

Summary for 2BE4

• Entry DOI: 10.2210/pdb2be4/pdb
• Descriptor: hypothetical protein LOC449832 (2 entities in total)
• Functional Keywords: dr.36843, bc083168, calicium binding, ef-hand superfamily, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, unknown function
• Biological source: Danio rerio (zebrafish)
• Cellular location: Cytoplasm : Q5XJX1
• Total number of polymer chains: 1
• Total formula weight: 32050.05

Authors

Wesenberg, G.E.,Phillips Jr., G.N.,Han, B.W.,Bitto, E.,Bingman, C.A.,Bae, E.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-10-21, release date: 2005-11-01, Last modification date: 2024-10-30)

Primary citation

Bitto, E.,Bingman, C.A.,Bittova, L.,Frederick, R.O.,Fox, B.G.,Phillips Jr., G.N.
X-ray structure of Danio rerio secretagogin: A hexa-EF-hand calcium sensor.
Proteins, 76:477-483, 2009

PubMed 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.

PubMed: 19241471
DOI: 10.1002/prot.22362

Experimental method

X-RAY DIFFRACTION (2.1 Å)