1PXE

Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1

Summary for 1PXE

• Entry DOI: 10.2210/pdb1pxe/pdb
• NMR Information: BMRB: 5901
• Descriptor: neural zinc finger transcription factor 1, ZINC ION (2 entities in total)
• Functional Keywords: cchhc zinc binding domain, neural zinc finger factor-1, dna binding domain, metal binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus: P70475
• Total number of polymer chains: 1
• Total formula weight: 7201.61

Authors

Berkovits-Cymet, H.J.,Amann, B.T.,Berg, J.M. (deposition date: 2003-07-03, release date: 2004-02-10, Last modification date: 2024-05-22)

Primary citation

Berkovits-Cymet, H.J.,Amann, B.T.,Berg, J.M.
Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1 and Its Implications for DNA Binding.
Biochemistry, 43:898-903, 2004

PubMed Abstract: The structure of a CCHHC zinc-binding domain from neural zinc finger factor-1 (NZF-1) has been determined in solution though the use of NMR methods. This domain is a member of a family of domains that have the Cys-X(4)-Cys-X(4)-His-X(7)-His-X(5)-Cys consensus sequence. The structure determination reveals a novel fold based around a zinc(II) ion coordinated to three Cys residues and the second of the two conserved His residues. The other His residue is stacked between the metal-coordinated His residue and a relatively conserved aromatic residue. Analysis of His to Gln sequence variants reveals that both His residues are required for the formation of a well-defined structure, but neither is required for high-affinity metal binding at a tetrahedral site. The structure suggests that a two-domain protein fragment and a double-stranded DNA binding site may interact with a common two-fold axis relating the two domains and the two half-sites of the DNA-inverted repeat.

PubMed: 14744132

Experimental method

SOLUTION NMR