6W9N
Solution structure of the FYVE domain of ALFY
Summary for 6W9N
| Entry DOI | 10.2210/pdb6w9n/pdb |
| NMR Information | BMRB: 30736 |
| Descriptor | WD repeat and FYVE domain-containing protein 3, ZINC ION (2 entities in total) |
| Functional Keywords | fyve domain, phosphoinositide binding, zinc binding, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9070.89 |
| Authors | Reinhart, E.F.,Pellegrini, M.,Ragusa, M.J. (deposition date: 2020-03-23, release date: 2020-12-23, Last modification date: 2024-05-15) |
| Primary citation | Reinhart, E.F.,Litt, N.A.,Katzenell, S.,Pellegrini, M.,Yamamoto, A.,Ragusa, M.J. A highly conserved glutamic acid in ALFY inhibits membrane binding to aid in aggregate clearance. Traffic, 22:23-37, 2021 Cited by PubMed Abstract: Autophagy-linked FYVE protein (ALFY) is a large, multidomain protein involved in the degradation of protein aggregates by selective autophagy. The C-terminal FYVE domain of ALFY has been shown to bind phosphatidylinositol 3-phosphate (PI(3)P); however, ALFY only partially colocalizes with other FYVE domains in cells. Thus, we asked if the FYVE domain of ALFY has distinct membrane binding properties compared to other FYVE domains and whether these properties might affect its function in vivo. We found that the FYVE domain of ALFY binds weakly to PI(3)P containing membranes in vitro. This weak binding is the result of a highly conserved glutamic acid within the membrane insertion loop in the FYVE domain of ALFY that is not present in any other human FYVE domain. In addition, not only does this glutamic acid reduce binding to membranes in vitro and inhibits its targeting to membranes in vivo, but it is also important for the ability of ALFY to clear protein aggregates. PubMed: 33225481DOI: 10.1111/tra.12771 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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