4EVU

Crystal structure of C-terminal domain of putative periplasmic protein ydgH from S. enterica

Summary for 4EVU

• Entry DOI: 10.2210/pdb4evu/pdb
• Descriptor: Putative periplasmic protein ydgH, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, psi-biology, program for the characterization of secreted effector proteins, pcsep, midwest center for structural genomics, mcsg, secreted effector, unknown function
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 2
• Total formula weight: 16747.32

Authors

Michalska, K.,Cui, H.,Xu, X.,Brown, R.N.,Cort, J.R.,Heffron, F.,Nakayasu, E.S.,Savchenko, A.,Adkins, J.N.,Joachimiak, A.,Program for the Characterization of Secreted Effector Proteins (PCSEP),Midwest Center for Structural Genomics (MCSG) (deposition date: 2012-04-26, release date: 2012-05-30, Last modification date: 2024-10-16)

Primary citation

Eletsky, A.,Michalska, K.,Houliston, S.,Zhang, Q.,Daily, M.D.,Xu, X.,Cui, H.,Yee, A.,Lemak, A.,Wu, B.,Garcia, M.,Burnet, M.C.,Meyer, K.M.,Aryal, U.K.,Sanchez, O.,Ansong, C.,Xiao, R.,Acton, T.B.,Adkins, J.N.,Montelione, G.T.,Joachimiak, A.,Arrowsmith, C.H.,Savchenko, A.,Szyperski, T.,Cort, J.R.
Structural and Functional Characterization of DUF1471 Domains of Salmonella Proteins SrfN, YdgH/SssB, and YahO.
Plos One, 9:e101787-e101787, 2014

PubMed 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.

PubMed: 25010333
DOI: 10.1371/journal.pone.0101787

Experimental method

X-RAY DIFFRACTION (1.45 Å)