1ZR9

Solution Structure of a Human C2H2-type Zinc Finger Protein

Summary for 1ZR9

• Entry DOI: 10.2210/pdb1zr9/pdb
• NMR Information: BMRB: 6682
• Descriptor: Zinc finger protein 593, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, dna binding, structural genomics, psi, protein structure initiative, center for eukaryotic structural genomics, cesg, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleolus: O00488
• Total number of polymer chains: 1
• Total formula weight: 14255.30

Authors

Lytle, B.L.,Peterson, F.C.,Volkman, B.F.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-05-19, release date: 2005-06-07, Last modification date: 2024-05-22)

Primary citation

Hayes, P.L.,Lytle, B.L.,Volkman, B.F.,Peterson, F.C.
The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein.
Protein Sci., 17:571-576, 2008

PubMed 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.

PubMed: 18287285
DOI: 10.1110/ps.073290408

Experimental method

SOLUTION NMR