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- Title
LUD, a new protein domain associated with lactate utilization.
- Authors
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
- Abstract
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.
- Subjects
PROTEINS; LACTATES; CRYSTAL structure; DEINOCOCCUS radiodurans; COFACTORS (Biochemistry); ENTEROTYPES
- Publication
BMC Bioinformatics, 2013, Vol 14, Issue 1, p1
- ISSN
1471-2105
- Publication type
Article
- DOI
10.1186/1471-2105-14-341