FEBS Letters
Volume 582, Issue 28 , Pages 3941-3947, 26 November 2008

Structural characterization of soluble E-Syt2

Edited by Maurice Mortal

  • Gerhard J. Groer

      Affiliations

    • Mikrobiologisches Institut – Klinische Mikrobiologie, Immunologie und Hygiene, Universitätsklinikum Erlangen, Wasserturmstraße 3-5, D-91054 Erlangen, Germany
    • ,
  • Martin Haslbeck

      Affiliations

    • Department Chemie, Technische Universität München, Lichtenbergstraße 4, D-85747 Garching, Germany
    • ,
  • Manfred Roessle

      Affiliations

    • European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestraße 85, D-22603 Hamburg, Germany
    • ,
  • André Gessner

      Affiliations

    • Mikrobiologisches Institut – Klinische Mikrobiologie, Immunologie und Hygiene, Universitätsklinikum Erlangen, Wasserturmstraße 3-5, D-91054 Erlangen, Germany
    • Corresponding Author InformationCorresponding author. Fax: +49 9131 85 25991.

Received 16 September 2008; received in revised form 17 October 2008; accepted 22 October 2008. published online 31 October 2008.

Abstract 

The protein family of membrane-anchored extended synaptotagmin-like proteins (E-Syts) was recently discovered in humans. E-Syt1 to 3 each contain at least one transmembrane domain and three or five C2 domains. To investigate the whole C2 area of murine E-Syt2, highly pure recombinant E-Syt2 (rE-Syt2) covering all three C2 domains was isolated. The structure of rE-Syt2 was studied by small-angle X-ray scattering (SAXS) providing a three-dimensional image of a protein with three C2 domains. Calcium binding of rE-Syt2 triggered structural rearrangements and initiated reversible multimerization of the protein in vitro. Quantitative analysis of the calcium binding revealed an apparent binding constant of 100μM. This is the first structural study of a multi-C2 protein, presumably involved in Ca-dependent signalling events.

Abbreviations: CD, circular dichroism, E-Syts, extended synaptotagmin-like proteins, PKC, protein kinase C, PLA, phospholipase A, PLC, phospholipase C, SAXS, small-angle X-ray scattering, SEC, size exclusion chromatography, SMP, synaptotagmin-like mitochondrial and lipid binding proteins, TM, transmembrane domain

Keywords: E-Syt2, C2 domain, Calcium binding, Multimerization, SAXS

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PII: S0014-5793(08)00870-3

doi:10.1016/j.febslet.2008.10.038

FEBS Letters
Volume 582, Issue 28 , Pages 3941-3947, 26 November 2008

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