Structural basis of ligand recognition and transport by Sfh2, a yeast phosphatidylinositol transfer protein of the Sec14 superfamily

Chen, L.; Tan, L.; Im, Y.J.

doi:10.1107/S2059798322005666

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 8
(a) Structural comparison of Sfh2–squalene and SPF–squalene. (b) The hydrophobic cavity of Sfh2 is shown as a transparent surface. Squalene is shown as yellow sticks. The two bulky residues in the center of the cavity are shown as stick models. (c) The hydrophobic cavity of SPF is shown as a transparent surface. Squalene is shown as gray sticks. (d) Structural comparison of the ligand-binding sites of Sfh2–squalene and Sfh1–PC (PDB entry 3b7z). The key residues of Sfh1 interacting with the PC head group are shown as stick models. The equivalent residues of Sfh2 are shown.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 7| July 2022| Pages 853-864

https://doi.org/10.1107/S2059798322005666

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page