PDBsum entry 2wt7

Transcription

PDB id: 2wt7

Contents

Protein chains

63 a.a. *

90 a.a. *

DNA/RNA

Ligands

PO4

Waters ×172

* Residue conservation analysis

PDB id:

2wt7

Name:

Transcription

Title:

Crystal structure of the bzip heterodimeric complex mafb:cfos bound to DNA

Structure:

Proto-oncogene protein c-fos. Chain: a. Fragment: residues 138-200. Synonym: cfos, cellular oncogene fos. Engineered: yes. Transcription factor mafb. Chain: b. Fragment: residues 214-303. Synonym: mafb, maf-b, v-maf musculoaponeurotic fibrosarcoma oncogene

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codon plus ril. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.

Resolution:

2.30Å R-factor: 0.230 R-free: 0.256

Authors:

V.Pogenberg,S.Holton,M.Wilmanns

Key ref:

V.Pogenberg et al. (2014). Design of a bZip transcription factor with homo/heterodimer-induced DNA-binding preference. Structure, 22, 466-477. PubMed id: 24530283 DOI: 10.1016/j.str.2013.12.017

Date:

11-Sep-09 Release date: 29-Sep-10

Protein chain

P01101  (FOS_MOUSE) -  Protein c-Fos from Mus musculus

Seq: 380 a.a.

Struc: 63 a.a.

Protein chain

P54841  (MAFB_MOUSE) -  Transcription factor MafB from Mus musculus

Seq: 323 a.a.

Struc: 90 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DNA/RNA chains

A-A-T-T-G-C-T-G-A-C-T-C-A-T-A-G 16 bases

C-T-A-T-G-A-G-T-C-A-G-C-A-A-T-T 16 bases

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/j.str.2013.12.017

Structure 22:466-477 (2014)

PubMed id: 24530283

Design of a bZip transcription factor with homo/heterodimer-induced DNA-binding preference.

V.Pogenberg, L.Consani Textor, L.Vanhille, S.J.Holton, M.H.Sieweke, M.Wilmanns.

ABSTRACT

The ability of basic leucine zipper transcription factors for homo- or heterodimerization provides a paradigm for combinatorial control of eukaryotic gene expression. It has been unclear, however, how facultative dimerization results in alternative DNA-binding repertoires on distinct regulatory elements. To unravel the molecular basis of such coupled preferences, we determined two high-resolution structures of the transcription factor MafB as a homodimer and as a heterodimer with c-Fos bound to variants of the Maf-recognition element. The structures revealed several unexpected and dimer-specific coiled-coil-heptad interactions. Based on these findings, we have engineered two MafB mutants with opposite dimerization preferences. One of them showed a strong preference for MafB/c-Fos heterodimerization and enabled selection of heterodimer-favoring over homodimer-specific Maf-recognition element variants. Our data provide a concept for transcription factor design to selectively activate dimer-specific pathways and binding repertoires.