PDBsum entry 1zr9

Transcription

PDB id: 1zr9

Contents

Protein chain

67 a.a. *

Metals

_ZN

* Residue conservation analysis

PDB id:

1zr9

Name:

Transcription

Title:

Solution structure of a human c2h2-type zinc finger protein

Structure:

Zinc finger protein 593. Chain: a. Synonym: zinc finger protein t86, zinc finger protein loc51042. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: znf593. Expressed in: cell-free synthesis. Other_details: wheat germ cell-free, in vitro expression

NMR struc:

20 models

Authors:

B.L.Lytle,F.C.Peterson,B.F.Volkman,Center For Eukaryotic Structural Genomics (Cesg)

Key ref:

P.L.Hayes et al. (2008). The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein. Protein Sci, 17, 571-576. PubMed id: 18287285 DOI: 10.1110/ps.073290408

Date:

19-May-05 Release date: 07-Jun-05

Protein chain

O00488  (ZN593_HUMAN) -  Zinc finger protein 593 from Homo sapiens

Seq: 134 a.a.

Struc: 67 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.073290408

Protein Sci 17:571-576 (2008)

PubMed id: 18287285

The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein.

P.L.Hayes, B.L.Lytle, B.F.Volkman, F.C.Peterson.

ABSTRACT

Here, we report the solution structure of ZNF593, a protein identified in a functional study as a negative modulator of the DNA-binding activity of the Oct-2 transcription factor. ZNF593 contains a classic C(2)H(2) zinc finger domain flanked by about 40 disordered residues on each terminus. Although the protein contains a high degree of intrinsic disorder, the structure of the zinc finger domain was resolved by NMR spectroscopy without a need for N- or C-terminal truncations. The tertiary structure of the zinc finger domain is composed of a beta-hairpin that positions the cysteine side chains for zinc coordination, followed by an atypical kinked alpha-helix containing the two histidine side chain ligands. The structural topology of ZNF593 is similar to a fragment of the double-stranded RNA-binding protein Zfa and the C-terminal zinc finger of MBP-1, a human enhancer binding protein. The structure presented here will provide a guide for future functional studies of how ZNF593 negatively modulates the DNA-binding activity of Oct-2, a POU domain-containing transcription factor. Our work illustrates the unique capacity of NMR spectroscopy for structural analysis of folded domains in a predominantly disordered protein.

Selected figure(s)

Figure 1.
(A) Two-dimensional ^15N --^1H HSQC spectrum of ZNF593 before (black contours) and after (red contours) the addition of 2 mM EDTA. Resonance assignments are indicated by a one-letter amino acid code followed by the specified residue number. (B) Ensemble of 20 conformers of ZNF593. (Gray) The N- and C-terminal unstructured regions (residues 28 --42 and 76 --94), (green) [beta]-sheet, (orange) [alpha]-helices, (green sphere) the zinc ion. (C) Cross-eyed stereoview of ZNF593, with unstructured residues 1 --35 and 78 --116 omitted for clarity. (D) Backbone r.m.s.d. and ^15N --^1H heteronuclear NOEs values displayed as a function of amino acid sequence. Locations of secondary structure elements are indicated.

Figure 2.
(A) Ribbon diagrams of ZNF593 (PDB code: 1zr9), the second zinc finger of dsRNA-ZFa (residues 94 --128) (PDB code: 1zu1), the C-terminal zinc finger of MBP-1 (residues 30 --57) (PDB code: 1bbo), and ZFY-swap (PDB code: 7znf). (B) Multiple sequence alignments demonstrating residue conservation between similar zinc fingers. (Green residues) Conserved amino acids. (C) Positively charged residues located on the solvent-exposed side of the [alpha]-helix are compared between ZNF593 and double-stranded RNA-binding protein ZFa.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2008, 17, 571-576) copyright 2008.