|Title||Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.|
|Publication Type||Journal Article|
|Year of Publication||2003|
|Authors||Ladner, JE, Obmolova, G, Teplyakov, A, Howard, AJ, Khil, PP, R Camerini-Otero, D, Gilliland, GL|
|Journal||BMC Struct Biol|
|Date Published||2003 Sep 30|
|Keywords||Binding Sites, Crystallography, X-Ray, Dimerization, Escherichia coli Proteins, Metals, Models, Molecular|
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.
|Alternate Journal||BMC Struct. Biol.|
|PubMed Central ID||PMC239858|
|Grant List||P01-GM57890 / GM / NIGMS NIH HHS / United States|