PDBsum entry 4xai

Transcription

PDB id: 4xai

Contents

Protein chains

565 a.a.

21 a.a.

18 a.a.

Ligands

GLC-GLC ×2

Waters ×86

PDB id:

4xai

Name:

Transcription

Title:

Crystal structure of red flour beetle nr2e1/tlx

Structure:

Maltose-binding periplasmic protein,tailless ortholog. Chain: a, b. Fragment: maltose binding protein fused ligand binding domain,maltose binding protein fused ligand binding domain. Synonym: mbp,mmbp,maltodextrin-binding protein. Engineered: yes. Grunge, isoform j. Chain: p, q. Fragment: atro box motif.

Source:

Escherichia coli o157:h7, tribolium castaneum. Red flour beetle. Organism_taxid: 83334, 7070. Gene: male, z5632, ecs5017. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Drosophila melanogaster. Fruit fly.

Resolution:

2.60Å R-factor: 0.211 R-free: 0.262

Authors:

X.Zhi,E.Zhou,E.Xu

Key ref:

X.Zhi et al. (2015). Structural basis for corepressor assembly by the orphan nuclear receptor TLX. Genes Dev, 29, 440-450. PubMed id: 25691470 DOI: 10.1101/gad.254904.114

Date:

14-Dec-14 Release date: 04-Mar-15

Protein chains

P0AEY0  (MALE_ECO57) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli O157:H7

Seq: 396 a.a.

Struc: 565 a.a.*

Protein chains

Q9NCL0  (Q9NCL0_TRICA) -  Tailless ortholog from Tribolium castaneum

Seq: 406 a.a.

Struc: 565 a.a.*

Protein chain

M9PHT1  (M9PHT1_DROME) -  Grunge, isoform J from Drosophila melanogaster

Seq: 2007 a.a.

Struc: 21 a.a.

Protein chain

M9PHT1  (M9PHT1_DROME) -  Grunge, isoform J from Drosophila melanogaster

Seq: 2007 a.a.

Struc: 18 a.a.

* PDB and UniProt seqs differ at 190 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains P, Q: E.C.3.5.1.- - ?????

DOI no: 10.1101/gad.254904.114

Genes Dev 29:440-450 (2015)

PubMed id: 25691470

Structural basis for corepressor assembly by the orphan nuclear receptor TLX.

X.Zhi, X.E.Zhou, Y.He, K.Searose-Xu, C.L.Zhang, C.C.Tsai, K.Melcher, H.E.Xu.

ABSTRACT

The orphan nuclear receptor TLX regulates neural stem cell self-renewal in the adult brain and functions primarily as a transcription repressor through recruitment of Atrophin corepressors, which bind to TLX via a conserved peptide motif termed the Atro box. Here we report crystal structures of the human and insect TLX ligand-binding domain in complex with Atro box peptides. In these structures, TLX adopts an autorepressed conformation in which its helix H12 occupies the coactivator-binding groove. Unexpectedly, H12 in this autorepressed conformation forms a novel binding pocket with residues from helix H3 that accommodates a short helix formed by the conserved ALXXLXXY motif of the Atro box. Mutations that weaken the TLX-Atrophin interaction compromise the repressive activity of TLX, demonstrating that this interaction is required for Atrophin to confer repressor activity to TLX. Moreover, the autorepressed conformation is conserved in the repressor class of orphan nuclear receptors, and mutations of corresponding residues in other members of this class of receptors diminish their repressor activities. Together, our results establish the functional conservation of the autorepressed conformation and define a key sequence motif in the Atro box that is essential for TLX-mediated repression.