4UUT
Crystal structure of the Ultrabithorax protein
Summary for 4UUT
| Entry DOI | 10.2210/pdb4uut/pdb |
| Related | 4UUS |
| Descriptor | HOMEOTIC PROTEIN ULTRABITHORAX, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | transcription, ubx, homeotic protein, transcription factor |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Cellular location | Nucleus: P83949 |
| Total number of polymer chains | 1 |
| Total formula weight | 11914.40 |
| Authors | Foos, N.,Mate, M.J.,Ortiz-Lombardia, M. (deposition date: 2014-07-31, release date: 2015-02-18, Last modification date: 2024-05-01) |
| Primary citation | Foos, N.,Maurel-Zaffran, C.,Mate, M.J.,Vincentelli, R.,Hainaut, M.,Berenger, H.,Pradel, J.,Saurin, A.J.,Ortiz-Lombardia, M.,Graba, Y. A Flexible Extension of the Drosophila Ultrabithorax Homeodomain Defines a Novel Hox/Pbc Interaction Mode. Structure, 23:270-, 2015 Cited by PubMed Abstract: The patterning function of Hox proteins relies on assembling protein complexes with PBC proteins, which often involves a protein motif found in most Hox proteins, the so-called Hexapeptide (HX). Hox/PBC complexes likely gained functional diversity by acquiring additional modes of interaction. Here, we structurally characterize the first HX alternative interaction mode based on the paralogue-specific UbdA motif and further functionally validate structure-based predictions. The UbdA motif folds as a flexible extension of the homeodomain recognition helix and defines Hox/PBC contacts that occur, compared with those mediated by the HX motif, on the opposing side of the DNA double helix. This provides a new molecular facet to Hox/PBC complex assembly and suggests possible mechanisms for the diversification of Hox protein function. PubMed: 25651060DOI: 10.1016/J.STR.2014.12.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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