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PLoS One. 2014 Jul 10;9(7):e101787. doi: 10.1371/journal.pone.0101787. eCollection 2014.

Structural and functional characterization of DUF1471 domains of Salmonella proteins SrfN, YdgH/SssB, and YahO.

Author information

1
Department of Chemistry, The State University of New York at Buffalo, Buffalo, New York, United States of America; Northeast Structural Genomics Consortium.
2
Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, United States of America; Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, United States of America.
3
Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada; Northeast Structural Genomics Consortium.
4
Fundamental and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, Washington, United States of America.
5
Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada; Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, United States of America.
6
Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America; Northeast Structural Genomics Consortium.
7
Department of Chemical Engineering and Applied Chemistry, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada; Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, United States of America.

Abstract

Bacterial species in the Enterobacteriaceae typically contain multiple paralogues of a small domain of unknown function (DUF1471) from a family of conserved proteins also known as YhcN or BhsA/McbA. Proteins containing DUF1471 may have a single or three copies of this domain. Representatives of this family have been demonstrated to play roles in several cellular processes including stress response, biofilm formation, and pathogenesis. We have conducted NMR and X-ray crystallographic studies of four DUF1471 domains from Salmonella representing three different paralogous DUF1471 subfamilies: SrfN, YahO, and SssB/YdgH (two of its three DUF1471 domains: the N-terminal domain I (residues 21-91), and the C-terminal domain III (residues 244-314)). Notably, SrfN has been shown to have a role in intracellular infection by Salmonella Typhimurium. These domains share less than 35% pairwise sequence identity. Structures of all four domains show a mixed α+β fold that is most similar to that of bacterial lipoprotein RcsF. However, all four DUF1471 sequences lack the redox sensitive cysteine residues essential for RcsF activity in a phospho-relay pathway, suggesting that DUF1471 domains perform a different function(s). SrfN forms a dimer in contrast to YahO and SssB domains I and III, which are monomers in solution. A putative binding site for oxyanions such as phosphate and sulfate was identified in SrfN, and an interaction between the SrfN dimer and sulfated polysaccharides was demonstrated, suggesting a direct role for this DUF1471 domain at the host-pathogen interface.

PMID:
25010333
PMCID:
PMC4092069
DOI:
10.1371/journal.pone.0101787
[Indexed for MEDLINE]
Free PMC Article

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