1JOC

EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate

Summary for 1JOC

• Entry DOI: 10.2210/pdb1joc/pdb
• Descriptor: Early Endosomal Autoantigen 1, ZINC ION, PHOSPHORIC ACID MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL) ESTER, ... (4 entities in total)
• Functional Keywords: fyve domain, inositol 3-phosphate binding, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q15075
• Total number of polymer chains: 2
• Total formula weight: 29220.02

Authors

Dumas, J.J.,Merithew, E.,Rajamani, D.,Hayes, S.,Lawe, D.,Corvera, S.,Lambright, D.G. (deposition date: 2001-07-27, release date: 2001-12-28, Last modification date: 2024-02-07)

Primary citation

Dumas, J.J.,Merithew, E.,Sudharshan, E.,Rajamani, D.,Hayes, S.,Lawe, D.,Corvera, S.,Lambright, D.G.
Multivalent endosome targeting by homodimeric EEA1.
Mol.Cell, 8:947-958, 2001

PubMed Abstract: Early endosome autoantigen localization to early endosomes is mediated by a C-terminal region, which includes a calmodulin binding motif, a Rab5 interaction site, and a FYVE domain that selectively binds phosphatidyl inositol 3-phosphate. The crystal structure of the C-terminal region bound to inositol 1,3-bisphosphate reveals an organized, quaternary assembly consisting of a parallel coiled coil and a dyad-symmetric FYVE domain homodimer. Structural and biochemical observations support a multivalent mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and modest specificity of head group interactions with conserved residues. A unique mode of membrane engagement deduced from the quaternary structure of the C-terminal region provides insight into the structural basis of endosome tethering.

PubMed: 11741531
DOI: 10.1016/S1097-2765(01)00385-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)