Solution Structure of a Zap1 Zinc-Responsive Domain Provides Insights into
Metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
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Solution structure of a Zap1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae.

Zap1 gene derived from pYeF2ZAP1 (gift from D.J. Eide, U Wisconsin-Madison). zzf1-2 portion of gene cloned into pET-21a plasmid (Novagen). Further details could be found in the entry citation.

Two zinc fingers that form an unusual stable interacting motif similar to F1-2 of GLI

Structural isoform of the current wild type protein shown to be suitable for structure calculations

The first zinc finger and with the interfinger linker of the current wild type protein

structural comparison of one- and two-zinc finger protein domains using chemical
shift data, in which the two fingers form a stable interacting motif

comparison of one- and two-zinc finger protein domains

Assignments for two-zinc finger protein of Zap1
backbone and side chain resonance assignments for zinc fingers 1 and 2 of Zap1 from Saccharomyces cerevisiae. Three non-zinc-liganding cysteines were mutated to alanines in order to obtain a stable protein for NMR data collection.
backbone resonance assignments for zinc finger 1 and a C-terminal disordered linker region of the Zap1 protein from Saccharomyces cerevisiae.