4CYC

CRYSTAL STRUCTURE OF A UBX-EXD-DNA COMPLEX INCLUDING THE HEXAPEPTIDE AND UBDA MOTIFS

Summary for 4CYC

• Entry DOI: 10.2210/pdb4cyc/pdb
• Descriptor: HOMEOTIC PROTEIN ULTRABITHORAX, HOMEOBOX PROTEIN EXTRADENTICLE, 5'-D(*GP*TP*CP*GP*CP*CP*AP*TP*AP*AP*AP*TP*CP*AP*CP)-3', ... (5 entities in total)
• Functional Keywords: transcription, hox, pbc, dna protein complex
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY); More
• Cellular location: Nucleus: P83949 P40427
• Total number of polymer chains: 4
• Total formula weight: 29495.19

Authors

Foos, N.,Mate, M.J.,Ortiz-Lombardia, M. (deposition date: 2014-04-10, release date: 2015-02-18, Last modification date: 2023-12-20)

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

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: 25651060
DOI: 10.1016/J.STR.2014.12.011

Experimental method

X-RAY DIFFRACTION (2.36 Å)