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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
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.
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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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