PDBsum entry 1fv5

Transcription

PDB id: 1fv5

Contents

Protein chain

36 a.a.

Metals

_ZN

PDB id:

1fv5

Name:

Transcription

Title:

Solution structure of the first zinc finger from the drosophila u- shaped transcription factor

Structure:

First zinc finger of u-shaped. Chain: a. Fragment: first zinc finger domain (residues 202-235). Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

C.K.Liew,K.Kowalski,A.H.Fox,A.Newton,B.K.Sharpe,M.Crossley,J.P.Mackay

Key ref:

C.K.Liew et al. (2000). Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions. Structure, 8, 1157-1166. PubMed id: 11080638 DOI: 10.1016/S0969-2126(00)00527-X

Date:

18-Sep-00 Release date: 04-Oct-00

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: E.C.?

DOI no: 10.1016/S0969-2126(00)00527-X

Structure 8:1157-1166 (2000)

PubMed id: 11080638

Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions.

C.K.Liew, K.Kowalski, A.H.Fox, A.Newton, B.K.Sharpe, M.Crossley, J.P.Mackay.

ABSTRACT

BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function.

Selected figure(s)

Figure 3.
Figure 3. Overlays of USH-F9 and the Sixth Finger from ZFYUSH-F9 is shown in blue, and the sixth finger from ZFY [23] is shown in red. The overlays are related by a 90° rotation about a horizontal axis in the plane of the page. The differences in side chain conformation in this region can be clearly seen

The above figure is reprinted by permission from Cell Press: Structure (2000, 8, 1157-1166) copyright 2000.

Figure was selected by the author.