PDBsum entry 4cyc

Transcription

PDB id: 4cyc

Contents

Protein chains

66 a.a.

58 a.a.

DNA/RNA

Waters ×68

PDB id:

4cyc

Name:

Transcription

Title:

Crystal structure of a ubx-exd-DNA complex including the hexapeptide and ubda motifs

Structure:

Homeotic protein ultrabithorax. Chain: a. Fragment: homeodomain with hx and ubda, residues 233-367. Engineered: yes. Homeobox protein extradenticle. Chain: b. Fragment: homeodomain residues 238-312. Synonym: dpbx, homeotic protein extradenticle. Engineered: yes.

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss. Synthetic: yes. Organism_taxid: 7227

Resolution:

2.36Å R-factor: 0.213 R-free: 0.227

Authors:

N.Foos,M.J.Mate,M.Ortiz-Lombardia

Key ref:

N.Foos et al. (2015). A flexible extension of the Drosophila ultrabithorax homeodomain defines a novel Hox/PBC interaction mode. Structure, 23, 270-279. PubMed id: 25651060 DOI: 10.1016/j.str.2014.12.011

Date:

10-Apr-14 Release date: 18-Feb-15

Protein chain

P83949  (UBX_DROME) -  Homeotic protein ultrabithorax from Drosophila melanogaster

Seq: 389 a.a.

Struc: 66 a.a.*

Protein chain

P40427  (EXD_DROME) -  Homeobox protein extradenticle from Drosophila melanogaster

Seq: 376 a.a.

Struc: 58 a.a.

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DNA/RNA chains

G-T-C-G-C-C-A-T-A-A-A-T-C-A-C 15 bases

A-C-G-T-G-A-T-T-T-A-T-G-G-C-G 15 bases

DOI no: 10.1016/j.str.2014.12.011

Structure 23:270-279 (2015)

PubMed id: 25651060

A flexible extension of the Drosophila ultrabithorax homeodomain defines a novel Hox/PBC interaction mode.

N.Foos, C.Maurel-Zaffran, M.J.Maté, R.Vincentelli, M.Hainaut, H.Berenger, J.Pradel, A.J.Saurin, M.Ortiz-Lombardía, Y.Graba.

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.