Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.

Printer-friendly versionPrinter-friendly versionPDF versionPDF version
TitleCrystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.
Publication TypeJournal Article
Year of Publication2003
AuthorsLadner, JE, Obmolova, G, Teplyakov, A, Howard, AJ, Khil, PP, R Camerini-Otero, D, Gilliland, GL
JournalBMC Struct Biol
Volume3
Pagination7
Date Published2003 Sep 30
ISSN1472-6807
KeywordsBinding Sites, Crystallography, X-Ray, Dimerization, Escherichia coli Proteins, Metals, Models, Molecular
Abstract

BACKGROUND: The protein encoded by the gene ybgI was chosen as a target for a structural genomics project emphasizing the relation of protein structure to function.

RESULTS: The structure of the ybgI protein is a toroid composed of six polypeptide chains forming a trimer of dimers. Each polypeptide chain binds two metal ions on the inside of the toroid.

CONCLUSION: The toroidal structure is comparable to that of some proteins that are involved in DNA metabolism. The di-nuclear metal site could imply that the specific function of this protein is as a hydrolase-oxidase enzyme.

DOI10.1186/1472-6807-3-7
Alternate JournalBMC Struct. Biol.
PubMed ID14519207
PubMed Central IDPMC239858
Grant ListP01-GM57890 / GM / NIGMS NIH HHS / United States