Structural Insights into the Mechanism of Protein O-Fucosylation POFUT1 Crystal Structure
2011

Understanding Protein O-Fucosylation Through the Crystal Structure of POFUT1

publication 10 minutes Evidence: high

Author Information

Author(s): Lira-Navarrete Erandi, Valero-González Jessika, Villanueva Raquel, Martínez-Júlvez Marta, Tejero Tomás, Merino Pedro, Panjikar Santosh, Hurtado-Guerrero Ramon

Primary Institution: University of Zaragoza

Hypothesis

What is the molecular mechanism of Protein O-fucosylation by POFUT1?

Conclusion

The study reveals the first crystal structure of POFUT1, providing insights into its catalytic mechanism and potential for inhibitor design.

Supporting Evidence

  • The crystal structure of POFUT1 was determined in both apo-form and in complex with GDP-fucose.
  • Mutagenesis studies identified Arg240 as a key residue for catalysis.
  • The study proposes a novel SN1-like catalytic mechanism for POFUT1.

Takeaway

Scientists studied a protein called POFUT1 that helps modify other proteins. They found out how it works and how it could help in making medicines.

Methodology

The researchers used X-ray crystallography to determine the structure of POFUT1 in different forms and conducted mutagenesis studies to identify key residues.

Limitations

The study primarily focuses on the crystal structure of POFUT1 from Caenorhabditis elegans, which may not fully represent the human enzyme.

Digital Object Identifier (DOI)

10.1371/journal.pone.0025365

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