3BD0
Crystal structure of Memo, form II
Summary for 3BD0
| Entry DOI | 10.2210/pdb3bd0/pdb |
| Related | 3BCZ |
| Descriptor | Protein MEMO1, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | alpha/beta structure, peptide binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 133244.45 |
| Authors | |
| Primary citation | Qiu, C.,Lienhard, S.,Hynes, N.E.,Badache, A.,Leahy, D.J. Memo Is Homologous to Nonheme Iron Dioxygenases and Binds an ErbB2-derived Phosphopeptide in Its Vestigial Active Site. J.Biol.Chem., 283:2734-2740, 2008 Cited by PubMed Abstract: Memo (mediator of ErbB2-driven cell motility) is a 297-amino-acid protein recently shown to co-precipitate with the C terminus of ErbB2 and be required for ErbB2-driven cell motility. Memo is not homologous to any known signaling proteins, and how it mediates ErbB2 signals is not known. To provide a molecular basis for understanding Memo function, we have determined and report here the 2.1A crystal structure of human Memo and show it be homologous to class III nonheme iron-dependent dioxygenases, a structural class that now includes a zinc-binding protein of unknown function. No metal binding or enzymatic activity can be detected for Memo, but Memo does bind directly to a specific ErbB2-derived phosphopeptide encompassing Tyr-1227 using its vestigial enzymatic active site. Memo thus represents a new class of phosphotyrosine-binding protein. PubMed: 18045866DOI: 10.1074/jbc.M703523200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.01 Å) |
Structure validation
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