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Related Experiment Videos

Mistletoe lectin I forms a double trefoil structure

E C Sweeney1, A G Tonevitsky, R A Palmer

  • 1Department of Crystallography, Birbeck College, University of London, UK.

FEBS Letters
|August 26, 1998
PubMed
Summary
This summary is machine-generated.

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Mistletoe lectin I (MLI) forms dimers through its B chains, a structure determined by X-ray crystallography. An evolutionary mutation in MLI

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular evolution

Background:

  • Mistletoe lectin I (MLI) is a type II ribosome-inactivating protein.
  • Understanding the quaternary structure of MLI is crucial for elucidating its biological function and interactions.
  • Ricin, a homologue of MLI, shares significant sequence homology but differs in its quaternary structure.

Purpose of the Study:

  • To determine the quaternary structure of Mistletoe Lectin I (MLI) using X-ray crystallography.
  • To investigate the molecular basis of MLI dimerization and compare it with ricin.
  • To explore the evolutionary implications of structural differences between MLI and ricin.

Main Methods:

  • X-ray crystallography was employed to determine the molecular structure of MLI.

Related Experiment Videos

  • Molecular replacement was utilized, with ricin coordinates serving as a search model.
  • Fast Protein Liquid Chromatography (FPLC) gel filtration was used to confirm dimerization in solution.

    • Main Results:

    • MLI exists as an [AB]2 dimer with internal two-fold symmetry.
    • The B chains of MLI dimerize via non-covalent interactions of looped chains, forming a double trefoil structure.
    • An evolutionary mutation (Cys39Ser) in MLI's alpha loop allows for the flexibility required for dimerization, unlike in ricin.

    Conclusions:

    • The quaternary structure of MLI is an [AB]2 dimer, stabilized by specific B-chain interactions.
    • The Cys39Ser mutation is key to MLI's dimerization capability and provides insight into ricin's monomeric nature.
    • MLI B-chain dimerization occurs in solution, with a measured association constant of 10(6) M.