6E8A

Crystal structure of DcrB from Salmonella enterica at 1.92 Angstroms resolution

Summary for 6E8A

• Entry DOI: 10.2210/pdb6e8a/pdb
• Descriptor: DUF1795 domain-containing protein (2 entities in total)
• Functional Keywords: mog1/psbp-like fold lipoprotein, unknown function
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 33932.29

Authors

Rasmussen, D.M.,Soens, R.W.,Bhattacharyya, B.,May, J.F. (deposition date: 2018-07-27, release date: 2018-10-31, Last modification date: 2024-03-13)

Primary citation

Rasmussen, D.M.,Soens, R.W.,Davie, T.J.,Vaneerd, C.K.,Bhattacharyya, B.,May, J.F.
The structure of DcrB, a lipoprotein from Salmonella enterica, reveals flexibility in the N-terminal segment of the Mog1p/PsbP-like fold.
J. Struct. Biol., 204:513-518, 2018

PubMed Abstract: DcrB is an 18 kDa 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 1.92 Å resolution by X-ray crystallography. This truncated form, DcrBΔ37, contains the entire domain of unknown function but lacks the lipoprotein signal sequence (residues 1-20) as well as residues 21-37. The DcrBΔ37 monomer contains the Mog1p/PsbP-like fold, which is found in functionally diverse proteins in mammals, yeast, plants, and cyanobacteria. Interestingly, DcrBΔ37 crystallized as a domain-swapped homodimer in which the N-terminal β-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.

PubMed: 30339832
DOI: 10.1016/j.jsb.2018.10.005

Experimental method

X-RAY DIFFRACTION (1.92 Å)