Structural highlights
FunctionESYT2_HUMAN May play a role as calcium-regulated intrinsic membrane protein.[1] Publication Abstract from PubMedContacts 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. Structure and Ca-Binding Properties of the Tandem C Domains of E-Syt2.,Xu J, Bacaj T, Zhou A, Tomchick DR, Sudhof TC, Rizo J Structure. 2013 Dec 24. pii: S0969-2126(13)00461-9. doi:, 10.1016/j.str.2013.11.011. PMID:24373768[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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