1HYI
SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN COMPLEXED WITH INOSITOL 1,3-BISPHOSPHATE
Summary for 1HYI
| Entry DOI | 10.2210/pdb1hyi/pdb |
| Related | 1HYJ |
| NMR Information | BMRB: 4579 |
| Descriptor | ENDOSOME-ASSOCIATED PROTEIN, ZINC ION, PHOSPHORIC ACID MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL) ESTER (3 entities in total) |
| Functional Keywords | beta sheet, alpha helix, zinc cluster, ptdins(3)p, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7703.23 |
| Authors | Kutateladze, T.,Overduin, M. (deposition date: 2001-01-19, release date: 2001-03-14, Last modification date: 2024-05-22) |
| Primary citation | Kutateladze, T.,Overduin, M. Structural mechanism of endosome docking by the FYVE domain. Science, 291:1793-1796, 2001 Cited by PubMed Abstract: The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines. PubMed: 11230696DOI: 10.1126/science.291.5509.1793 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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