Crystal structure of the PX domain of Vps17p from Saccharomyces cerevisiae

Takayuki Obita, Koji Inaka, Daisuke Kohda, Nobuo Maita

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


The structure determination of the PX (phox homology) domain of the Saccharomyces cerevisiae Vps17p protein presented a challenging case for molecular replacement because it has noncrystallographic symmetry close to a crystallographic axis. The combination of diffraction-quality crystals grown under microgravity on the International Space Station and a highly accurate template structure predicted by AlphaFold2 provided the key to successful crystal structure determination. Although the structure of the Vps17p PX domain is seen in many PX domains, no basic residues are found around the canonical phosphatidylinositol phosphate (PtdIns-P) binding site, suggesting an inability to bind PtdIns-P molecules.

Original languageEnglish
Pages (from-to)210-216
Number of pages7
JournalActa Crystallographica Section F: Structural Biology Communications
Publication statusPublished - May 1 2022

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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