2MA4

Solution NMR Structure of yahO protein from Salmonella typhimurium, Northeast Structural Genomics Consortium (NESG) Target StR106

2MA4 の概要

• エントリーDOI: 10.2210/pdb2ma4/pdb
• NMR情報: BMRB: 19327
• 分子名称: Putative periplasmic protein (1 entity in total)
• 機能のキーワード: structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative, duf1471, membrane protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8744.85

構造登録者

Eletsky, A.,Zhang, Q.,Liu, G.,Wang, H.,Nwosu, C.,Cunningham, K.,Ma, L.,Xiao, R.,Liu, J.,Baran, M.C.,Swapna, G.,Acton, T.B.,Rost, B.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2013-06-27, 公開日: 2013-08-28, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR