6IYY
Crystal structure of human WIPI3,loop deletion mutant
Summary for 6IYY
| Entry DOI | 10.2210/pdb6iyy/pdb |
| Descriptor | WD repeat domain phosphoinositide-interacting protein 3, SULFATE ION (3 entities in total) |
| Functional Keywords | membrane bound protein, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 35639.44 |
| Authors | Liang, R.B.,Ren, J.Q.,Feng, W. (deposition date: 2018-12-17, release date: 2019-03-13, Last modification date: 2024-03-27) |
| Primary citation | Liang, R.,Ren, J.,Zhang, Y.,Feng, W. Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI Proteins. J. Mol. Biol., 431:1494-1505, 2019 Cited by PubMed Abstract: WIPI proteins are mammalian PROPPIN family members that bind to phosphoinositides and play prominent roles in autophagosome biogenesis. Two phosphoinositide-binding sites were previously described in yeast PROPPIN Hsv2 but remain to be determined in mammalian WIPI proteins. Here, we characterized four human WIPI proteins (WIPI1-4) and solved the structure of WIPI3. WIPI proteins can bind to PI(3)P and PI(3,5)P and adopt a conventional seven-bladed β-propeller fold. The structure of WIPI3 revealed that WIPI proteins also contain two sites embedded in blades 5 and 6 for recognizing phosphoinositides, resembling that in Hsv2. Structural comparison further demonstrated that the two conserved phosphoinositide-binding sites in PROPPIN proteins are not identical but intrinsically tend to recognize different types of phosphoinositides. This work provides the structural evidence to support the conservation of the two phosphoinositide-binding sites in WIPI proteins and also uncovers the potential phosphoinositide-binding selectivity for each site. PubMed: 30797857DOI: 10.1016/j.jmb.2019.02.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.796 Å) |
Structure validation
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