1pxe
From Proteopedia
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Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1
Overview
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.
About this Structure
1PXE is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of a CCHHC domain of neural zinc finger factor-1 and its implications for DNA binding., Berkovits-Cymet HJ, Amann BT, Berg JM, Biochemistry. 2004 Feb 3;43(4):898-903. PMID:14744132
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