TY - JOUR
T1 - Crystal structure of the PX domain of Vps17p from Saccharomyces cerevisiae
AU - Obita, Takayuki
AU - Inaka, Koji
AU - Kohda, Daisuke
AU - Maita, Nobuo
N1 - Funding Information:
This work was supported by Japan Society for the Promotion of Science (JSPS) KAKENHI Grant No. JP21H02448 and Mitsubishi Foundation (Japan) Research Grants in the Natural Sciences Grant No. 202110017 to DK.
Publisher Copyright:
© 2022 International Union of Crystallography. All rights reserved.
PY - 2022/5/1
Y1 - 2022/5/1
N2 - 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.
AB - 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.
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U2 - 10.1107/S2053230X22004472
DO - 10.1107/S2053230X22004472
M3 - Article
C2 - 35506766
AN - SCOPUS:85129384477
SN - 1744-3091
VL - 78
SP - 210
EP - 216
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
ER -