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LUD, a new protein domain associated with lactate utilization
BACKGROUND: A novel highly conserved protein domain, DUF162 [Pfam: PF02589], can be mapped to two proteins: LutB and LutC. Both proteins are encoded by a highly conserved LutABC operon, which has been implicated in lactate utilization in bacteria. Based on our analysis of its sequence, structure, an...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3924224/ https://www.ncbi.nlm.nih.gov/pubmed/24274019 http://dx.doi.org/10.1186/1471-2105-14-341 |
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author | Hwang, William C Bakolitsa, Constantina Punta, Marco Coggill, Penelope C Bateman, Alex Axelrod, Herbert L Rawlings, Neil D Sedova, Mayya Peterson, Scott N Eberhardt, Ruth Y Aravind, L Pascual, Jaime Godzik, Adam |
author_facet | Hwang, William C Bakolitsa, Constantina Punta, Marco Coggill, Penelope C Bateman, Alex Axelrod, Herbert L Rawlings, Neil D Sedova, Mayya Peterson, Scott N Eberhardt, Ruth Y Aravind, L Pascual, Jaime Godzik, Adam |
author_sort | Hwang, William C |
collection | PubMed |
description | BACKGROUND: A novel highly conserved protein domain, DUF162 [Pfam: PF02589], can be mapped to two proteins: LutB and LutC. Both proteins are encoded by a highly conserved LutABC operon, which has been implicated in lactate utilization in bacteria. Based on our analysis of its sequence, structure, and recent experimental evidence reported by other groups, we hereby redefine DUF162 as the LUD domain family. RESULTS: JCSG solved the first crystal structure [PDB:2G40] from the LUD domain family: LutC protein, encoded by ORF DR_1909, of Deinococcus radiodurans. LutC shares features with domains in the functionally diverse ISOCOT superfamily. We have observed that the LUD domain has an increased abundance in the human gut microbiome. CONCLUSIONS: We propose a model for the substrate and cofactor binding and regulation in LUD domain. The significance of LUD-containing proteins in the human gut microbiome, and the implication of lactate metabolism in the radiation-resistance of Deinococcus radiodurans are discussed. |
format | Online Article Text |
id | pubmed-3924224 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-39242242014-02-15 LUD, a new protein domain associated with lactate utilization Hwang, William C Bakolitsa, Constantina Punta, Marco Coggill, Penelope C Bateman, Alex Axelrod, Herbert L Rawlings, Neil D Sedova, Mayya Peterson, Scott N Eberhardt, Ruth Y Aravind, L Pascual, Jaime Godzik, Adam BMC Bioinformatics Research Article BACKGROUND: A novel highly conserved protein domain, DUF162 [Pfam: PF02589], can be mapped to two proteins: LutB and LutC. Both proteins are encoded by a highly conserved LutABC operon, which has been implicated in lactate utilization in bacteria. Based on our analysis of its sequence, structure, and recent experimental evidence reported by other groups, we hereby redefine DUF162 as the LUD domain family. RESULTS: JCSG solved the first crystal structure [PDB:2G40] from the LUD domain family: LutC protein, encoded by ORF DR_1909, of Deinococcus radiodurans. LutC shares features with domains in the functionally diverse ISOCOT superfamily. We have observed that the LUD domain has an increased abundance in the human gut microbiome. CONCLUSIONS: We propose a model for the substrate and cofactor binding and regulation in LUD domain. The significance of LUD-containing proteins in the human gut microbiome, and the implication of lactate metabolism in the radiation-resistance of Deinococcus radiodurans are discussed. BioMed Central 2013-11-26 /pmc/articles/PMC3924224/ /pubmed/24274019 http://dx.doi.org/10.1186/1471-2105-14-341 Text en Copyright © 2013 Hwang et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Hwang, William C Bakolitsa, Constantina Punta, Marco Coggill, Penelope C Bateman, Alex Axelrod, Herbert L Rawlings, Neil D Sedova, Mayya Peterson, Scott N Eberhardt, Ruth Y Aravind, L Pascual, Jaime Godzik, Adam LUD, a new protein domain associated with lactate utilization |
title | LUD, a new protein domain associated with lactate utilization |
title_full | LUD, a new protein domain associated with lactate utilization |
title_fullStr | LUD, a new protein domain associated with lactate utilization |
title_full_unstemmed | LUD, a new protein domain associated with lactate utilization |
title_short | LUD, a new protein domain associated with lactate utilization |
title_sort | lud, a new protein domain associated with lactate utilization |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3924224/ https://www.ncbi.nlm.nih.gov/pubmed/24274019 http://dx.doi.org/10.1186/1471-2105-14-341 |
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