Structure
Volume 22, Issue 2, 4 February 2014, Pages 269-280
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Article
Structure and Ca2+-Binding Properties of the Tandem C2 Domains of E-Syt2

https://doi.org/10.1016/j.str.2013.11.011Get rights and content
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Highlights

  • The crystal structure of the tandem C2AB domains of E-Syt2 has been determined

  • The structure has a V shape with a rigid orientation of the two C2 domains

  • The E-Syt2 C2A domain binds four Ca2+ ions, whereas the C2B domain does not bind Ca2+

  • E-Syts most likely have an as yet unidentified Ca2+-dependent function

Summary

Contacts between the endoplasmic reticulum and the plasma membrane involve extended synaptotagmins (E-Syts) in mammals or tricalbins in yeast, proteins with multiple C2 domains. One of the tandem C2 domains of E-Syt2 is predicted to bind Ca2+, but no Ca2+-dependent function has been attributed to this protein. We have determined the crystal structures of the tandem C2 domains of E-Syt2 in the absence and presence of Ca2+ and analyzed their Ca2+-binding properties by nuclear magnetic resonance spectroscopy. Our data reveal an unexpected V-shaped structure with a rigid orientation between the two C2 domains that is not substantially altered by Ca2+. The E-Syt2 C2A domain binds up to four Ca2+ ions, whereas the C2B domain does not bind Ca2+. These results suggest that E-Syt2 performs an as yet unidentified Ca2+-dependent function through its C2A domain and uncover fundamental differences between the properties of the tandem C2 domains of E-Syts and synaptotagmins.

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