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Structural elucidation of the PDI-related chaperone Wind with the help of mutants

Madhumati Sevvana1, Marianna Biadene, Qingjun Ma

  • 1Lehrstuhl für Strukturchemie, Georg-August Universität, Tammanstrasse 4, D-37077 Göttingen, Germany.

Acta Crystallographica. Section D, Biological Crystallography
|May 16, 2006
PubMed

Insights

The protein Wind forms dimers, which are likely its active form. Mutations affecting Pipe transport suggest altered binding interactions, impacting Wind

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The protein Wind, related to protein disulfide isomerase (PDI), plays a role in cellular transport.
  • Understanding Wind's structure and function is crucial for elucidating its biological mechanisms.

Purpose of the Study:

  • To determine and compare the structures of wild-type Wind and its mutants (Y53S, Y53F, Y55K).
  • To investigate the role of dimerization in Wind's function and its interaction with the protein Pipe.

Main Methods:

  • X-ray crystallography was used to determine the structures of Wind and its mutants.
  • Structural comparisons were made between wild-type and mutant forms.

Main Results:

  • All determined structures exhibited the same dimerization mode, independent of the His(6) tag position.
  • Mutants Y53S and Y55K abolished Pipe transport, despite subtle changes in the putative Pipe-binding region.
  • Active Wind binding to Pipe involves hydrophobic interactions, while inactive mutants may form stronger hydrogen bonds.

Conclusions:

  • Wind dimerization is likely a stable, biologically relevant feature.
  • Specific mutations disrupt Pipe transport by altering the binding interface, potentially through altered interaction types (hydrophobic vs. hydrogen bonding).
  • The findings provide insights into the mechanism of Wind-mediated Pipe transport and the structural basis of its regulation.

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