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Updated: Jun 28, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Structural characterization of soluble E-Syt2.

Gerhard J Groer1, Martin Haslbeck, Manfred Roessle

  • 1Mikrobiologisches Institut - Klinische Mikrobiologie, Immunologie und Hygiene, Universitätsklinikum Erlangen, Wasserturmstrasse 3-5, D-91054 Erlangen, Germany.

FEBS Letters
|November 4, 2008
PubMed
Summary
This summary is machine-generated.

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Researchers studied the structure of a mouse protein called extended synaptotagmin-like protein 2 (E-Syt2). They found that calcium binding causes E-Syt2 to change shape and form reversible multimers in vitro.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Cell Biology

Background:

  • Membrane-anchored extended synaptotagmin-like proteins (E-Syts) are a recently identified protein family in humans.
  • E-Syt proteins (E-Syt1 to E-Syt3) possess transmembrane domains and multiple C2 domains, suggesting roles in cellular signaling.
  • The specific functions and structural characteristics of E-Syt proteins, particularly multi-C2 domain proteins, remain largely unexplored.

Purpose of the Study:

  • To elucidate the three-dimensional structure of murine E-Syt2, focusing on its C2 domains.
  • To investigate the effects of calcium binding on the structure and behavior of recombinant E-Syt2 (rE-Syt2).
  • To characterize the calcium-binding properties and potential multimerization of rE-Syt2 in vitro.

Main Methods:

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Last Updated: Jun 28, 2026

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  • Isolation and purification of highly pure recombinant murine E-Syt2 (rE-Syt2) encompassing all three C2 domains.
  • Small-angle X-ray scattering (SAXS) to determine the overall three-dimensional structure of rE-Syt2.
  • In vitro assays to study calcium binding, structural rearrangements, and protein multimerization.

Main Results:

  • SAXS analysis provided a 3D structural model of rE-Syt2, revealing its multi-C2 domain architecture.
  • Calcium binding to rE-Syt2 induced significant structural rearrangements.
  • rE-Syt2 exhibited reversible multimerization in vitro upon calcium binding, with an apparent binding constant of approximately 100 μM.

Conclusions:

  • This study presents the first structural investigation of a multi-C2 domain E-Syt protein.
  • Calcium binding is a key regulator of E-Syt2 structure and function, promoting multimerization.
  • The findings suggest a role for E-Syt2 in calcium-dependent signaling pathways within the cell.