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BMC Bioinformatics. 2013 Nov 26;14:341. doi: 10.1186/1471-2105-14-341.

LUD, a new protein domain associated with lactate utilization.

Author information

1
Joint Center for Structural Genomics, La Jolla, CA 92037, USA. wchwang@sanfordburnham.org.

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.

PMID:
24274019
PMCID:
PMC3924224
DOI:
10.1186/1471-2105-14-341
[Indexed for MEDLINE]
Free PMC Article

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