NMR Structure of the Escherichia Coli Protein YacG; A Novel Sequence Motif in the Zinc-Finger Family of Proteins
- BATTELLE (PACIFIC NW LAB)
- Ontario Cancer Institute
- University of Toronto
- 9012
We have used nuclear magnetic resonance (NMR) spectroscopy to determine the solution structure of YacG (gi|7466984), a small zinc-binding protein encoded by the Escherichia coli yacG gene. YacG is a conserved hypothetical protein (COG 3024) with homologs in various bacterial species (Fig. 1). A structure similarity search using Dali1 did not reveal any structurally similar proteins (Z-score all < 2). However, the protein has characteristic features of a zinc finger including two antiparallel?O-strands, an??-helix, and a tetrahedral Zn+2 binding site. The consensus motif for the Cys residues (-C-X2-C-X15-C-X3-C-) is invariant among the YacG homologs, but is not present in any other zinc binding proteins with known structures.
- Research Organization:
- Pacific Northwest National Lab., Richland, WA (US), Environmental Molecular Sciences Lab. (US)
- Sponsoring Organization:
- US Department of Energy (US)
- DOE Contract Number:
- AC06-76RL01830
- OSTI ID:
- 15005572
- Report Number(s):
- PNWD-SA-5717; 2427; TRN: US200402%%123
- Journal Information:
- Proteins: Structure, Function, and Genetics, Vol. 49, Issue 2; Other Information: PBD: 1 Nov 2002
- Country of Publication:
- United States
- Language:
- English
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