PDBsum entry 1y0j

DNA binding protein

PDB id: 1y0j

Contents

Protein chains

39 a.a. *

36 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1y0j

Name:

DNA binding protein

Title:

Zinc fingers as protein recognition motifs: structural basis for the gata-1/friend of gata interaction

Structure:

Erythroid transcription factor. Chain: a. Fragment: gnf. Synonym: gata-1, eryf1, gf-1, nf-e1. Engineered: yes. Zinc-finger protein ush. Chain: b. Fragment: usf1. Synonym: u-shaped transcription factor, u-shaped protein.

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: gata-1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227.

NMR struc:

20 models

Authors:

C.K.Liew,R.J.Y.Simpson,A.H.Y.Kwan,L.A.Crofts,F.E.Loughlin, J.M.Matthews,M.Crossley,J.P.Mackay

Key ref:

C.K.Liew et al. (2005). Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction. Proc Natl Acad Sci U S A, 102, 583-588. PubMed id: 15644435 DOI: 10.1073/pnas.0407511102

Date:

15-Nov-04 Release date: 25-Jan-05

Protein chain

P17679  (GATA1_MOUSE) -  Erythroid transcription factor from Mus musculus

Seq: 413 a.a.

Struc: 39 a.a.

Protein chain

Q9VPQ6  (USH_DROME) -  Zinc finger protein ush from Drosophila melanogaster

Seq: 1191 a.a.

Struc: 36 a.a.*

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

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1073/pnas.0407511102

Proc Natl Acad Sci U S A 102:583-588 (2005)

PubMed id: 15644435

Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction.

C.K.Liew, R.J.Simpson, A.H.Kwan, L.A.Crofts, F.E.Loughlin, J.M.Matthews, M.Crossley, J.P.Mackay.

ABSTRACT

GATA-1 and friend of GATA (FOG) are zinc-finger transcription factors that physically interact to play essential roles in erythroid and megakaryocytic development. Several naturally occurring mutations in the GATA-1 gene that alter the FOG-binding domain have been reported. The mutations are associated with familial anemias and thrombocytopenias of differing severity. To elucidate the molecular basis for the GATA-1/FOG interaction, we have determined the three-dimensional structure of a complex comprising the interaction domains of these proteins. The structure reveals how zinc fingers can act as protein recognition motifs. Details of the architecture of the contact domains and their physical properties provide a molecular explanation for how the GATA-1 mutations contribute to distinct but related genetic diseases.

Selected figure(s)

Figure 2.
Fig. 2. The GATA-1:dFOG interface. Electrostatic surfaces of mNF (Left) and dFOG-F1 (Right) are shown (blue for mNF and red for dFOG-F1). The relative orientations of each image compared with Fig. 1 are indicated.

Figure 3.
Fig. 3. Sequence diversity in GATA-binding FOG ZnFs. (A) The GATA-FOG structure showing the position of A225[dFOG] (Left), and the likely position of the valine side chain that replaces A225 in a complex formed between NF and mFOG-F6 (Right). (B) Position of the S218 side chain and the two nearby glutamates from NF (Left). (Right) The likely position of the arginine side chain that would replace S218 in a NF/mFOG-F1 complex.

Figures were selected by an automated process.