PDBsum entry: 1gnf

Transcription regulation

PDB id: 1gnf

Contents

Protein chain

46 a.a. *

Metals

_ZN

* Residue conservation analysis

PDB id:

1gnf

Name:

Transcription regulation

Title:

Solution structure of the n-terminal zinc finger of murine gata-1, nmr, 25 structures

Structure:

Transcription factor gata-1. Chain: a. Fragment: n-terminal zinc finger. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

25 models

Authors:

K.Kowalski,R.Czolij,G.F.King,M.Crossley,J.P.Mackay

Key ref:

K.Kowalski et al. (1999). The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG. J Biomol Nmr, 13, 249-262. PubMed id: 10212985 DOI: 10.1023/A:1008309602929

Date:

12-Oct-98 Release date: 08-Jun-99

Protein chain

P17679  (GATA1_MOUSE) -  Erythroid transcription factor

Seq: 413 a.a.

Struc: 46 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: regulation of transcription, DNA-dependent (1 term)
• Biochemical function: transcription factor activity (3 terms)

DOI no: 10.1023/A:1008309602929

J Biomol Nmr 13:249-262 (1999)

PubMed id: 10212985

The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG.

K.Kowalski, R.Czolij, G.F.King, M.Crossley, J.P.Mackay.

ABSTRACT

Zinc fingers (ZnFs) are generally regarded as DNA-binding motifs. However, a number of recent reports have implicated particular ZnFs in the mediation of protein-protein interactions. The N-terminal ZnF of GATA-1 (NF) is one such finger, having been shown to interact with a number of other proteins, including the recently discovered transcriptional co-factor FOG. Here we solve the three-dimensional structure of the NF in solution using multidimensional 1H/15N NMR spectroscopy, and we use 1H/15N spin relaxation measurements to investigate its backbone dynamics. The structure consists of two distorted beta-hairpins and a single alpha-helix, and is similar to that of the C-terminal ZnF of chicken GATA-1. Comparisons of the NF structure with those of other C4-type zinc binding motifs, including hormone receptor and LIM domains, also reveal substantial structural homology. Finally, we use the structure to map the spatial locations of NF residues shown by mutagenesis to be essential for FOG binding, and demonstrate that these residues all lie on a single face of the NF. Notably, this face is well removed from the putative DNA-binding face of the NF, an observation which is suggestive of simultaneous roles for the NF; that is, stabilisation of GATA-1 DNA complexes and recruitment of FOG to GATA-1-controlled promoter regions.