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Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site
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...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239858/ https://www.ncbi.nlm.nih.gov/pubmed/14519207 http://dx.doi.org/10.1186/1472-6807-3-7 |
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author | Ladner, Jane E Obmolova, Galina Teplyakov, Alexey Howard, Andrew J Khil, Pavel P Camerini-Otero, R Daniel Gilliland, Gary L |
author_facet | Ladner, Jane E Obmolova, Galina Teplyakov, Alexey Howard, Andrew J Khil, Pavel P Camerini-Otero, R Daniel Gilliland, Gary L |
author_sort | Ladner, Jane E |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-239858 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-2398582003-11-04 Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site Ladner, Jane E Obmolova, Galina Teplyakov, Alexey Howard, Andrew J Khil, Pavel P Camerini-Otero, R Daniel Gilliland, Gary L BMC Struct Biol Research Article 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. BioMed Central 2003-09-30 /pmc/articles/PMC239858/ /pubmed/14519207 http://dx.doi.org/10.1186/1472-6807-3-7 Text en Copyright © 2003 Ladner et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. |
spellingShingle | Research Article Ladner, Jane E Obmolova, Galina Teplyakov, Alexey Howard, Andrew J Khil, Pavel P Camerini-Otero, R Daniel Gilliland, Gary L Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title | Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title_full | Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title_fullStr | Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title_full_unstemmed | Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title_short | Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site |
title_sort | crystal structure of escherichia coli protein ybgi, a toroidal structure with a dinuclear metal site |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239858/ https://www.ncbi.nlm.nih.gov/pubmed/14519207 http://dx.doi.org/10.1186/1472-6807-3-7 |
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