Unknown

Dataset Information

0

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


ABSTRACT: 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.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.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.

SUBMITTER: Ladner JE 

PROVIDER: S-EPMC239858 | biostudies-literature | 2003 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Ladner Jane E JE   Obmolova Galina G   Teplyakov Alexey A   Howard Andrew J AJ   Khil Pavel P PP   Camerini-Otero R Daniel RD   Gilliland Gary L GL  

BMC structural biology 20030930


<h4>Background</h4>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.<h4>Results</h4>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.<h4>Conclusion</h4>The toroidal structure is comparable to that of some proteins that are involved in DNA metabolism. The di-nuclear  ...[more]

Similar Datasets

| S-EPMC3078058 | biostudies-literature
| S-EPMC529075 | biostudies-literature
| S-EPMC2688778 | biostudies-literature
| S-EPMC3005795 | biostudies-literature
| S-EPMC4528939 | biostudies-literature
| S-EPMC2792208 | biostudies-literature
| S-EPMC4038516 | biostudies-literature
| S-EPMC2728841 | biostudies-literature
| S-EPMC2203310 | biostudies-literature
| S-EPMC2613045 | biostudies-literature