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Updated: Sep 16, 2025

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N‑Terminal Protein Complexation and Assembly with a Triangular Sulfated Macrocycle.

Marvin C Ifeagwu1, Lijuan Guo2, Niamh M Mockler1

  • 1School of Biological and Chemical Sciences, University of Galway, Galway H91 TK33, Ireland.

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|July 8, 2025
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Summary
This summary is machine-generated.

Researchers crystallized a mutant Ralstonia solanacearum lectin (RSL) with sulfated terphen[3]-arene (STP3). This revealed novel protein-binding interactions, offering insights into lectin-heparan sulfate binding and protein crystallization methods.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Crystallography

Background:

  • Ralstonia solanacearum lectin (RSL) is a protein with potential roles in molecular interactions.
  • Sulfated macrocycles are emerging as novel molecules with unique binding properties.
  • Understanding protein-ligand interactions is crucial for biochemistry and structural biology.

Purpose of the Study:

  • To elucidate the structural basis of RSL interaction with a novel sulfated macrocycle, STP3.
  • To explore the protein-binding modes and implications for crystal packing.
  • To investigate potential applications in protein assembly and understanding lectin-heparan sulfate interactions.

Main Methods:

  • X-ray crystallography was used to determine two cocrystal structures of mutant RSL with STP3.
  • Analysis of the crystal structures revealed specific binding interactions and their effect on crystal packing.

Main Results:

  • Two distinct binding modes of STP3 to RSL were identified: methionine encapsulation and insertion between surface loops.
  • The rigidity of the STP3 macrocycle was observed to facilitate crystal packing.
  • The observed interactions provide a structural basis for understanding lectin-macrocycle complex formation.

Conclusions:

  • The study presents novel cocrystal structures of RSL with STP3, detailing unique binding interactions.
  • STP3 demonstrates potential as a tool for protein assembly and crystallization.
  • The findings have implications for understanding lectin-heparan sulfate interactions in biological systems.