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Publication Abstract from PubMed

DcrB is an 18kDa lipoprotein that contains a single domain of unknown function. DcrB is found within Enterobacteriaceae, a family of Gram-negative bacteria which includes pathogens that can cause food-borne illness and hospital-acquired infections. In Salmonella enterica serovar Typhimurium, DcrB is up-regulated by conditions that promote the production of known virulence factors. We determined the structure of a truncated form of DcrB from Salmonella to 1.92A resolution by X-ray crystallography. This truncated form, DcrBDelta37, contains the entire domain of unknown function but lacks the lipoprotein signal sequence (residues 1-20) as well as residues 21-37. The DcrBDelta37 monomer contains the Mog1p/PsbP-like fold, which is found in functionally diverse proteins in mammals, yeast, plants, and cyanobacteria. Interestingly, DcrBDelta37 crystallized as a domain-swapped homodimer in which the N-terminal beta-hairpin extends from one protomer to interact with the core of the second protomer. This domain-swapping indicates that the N-terminal portion of the Mog1p/PsbP-like fold likely has conformational flexibility. Overall, our results provide the first example of an enterobacterial protein that contains the Mog1p/PsbP-like fold and expands knowledge of the structural and phylogenetic diversity of Mog1p/PsbP-like proteins.

The structure of DcrB, a lipoprotein from Salmonella enterica, reveals flexibility in the N-terminal segment of the Mog1p/PsbP-like fold.,Rasmussen DM, Soens RW, Davie TJ, Vaneerd CK, Bhattacharyya B, May JF J Struct Biol. 2018 Oct 16. pii: S1047-8477(18)30278-8. doi:, 10.1016/j.jsb.2018.10.005. PMID:30339832^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.