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Solution NMR structure of CHU_1110 from Cytophaga hutchinsonii , an AHSA1 protein potentially involved in metal ion stress response
Author(s) -
Liang Chunjie,
Zhu Jiang,
Ramelot Theresa A.,
Kennedy Michael A.,
Yue Xiali,
Li Xuegang,
Liu Maili,
He Ting,
Yang Yunhuang
Publication year - 2019
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25622
Subject(s) - antiparallel (mathematics) , chemistry , context (archaeology) , metal ions in aqueous solution , crystallography , cytophaga , metal , biochemistry , bacteria , stereochemistry , biology , genetics , organic chemistry , physics , pseudomonas , paleontology , flavobacterium , quantum mechanics , magnetic field
We report the solution nuclear magnetic resonance (NMR) structure of CHU_1110 from Cytophaga hutchinsonii . CHU_1110 contains three α‐helices and one antiparallel β‐sheet, forming a large cavity in the center of the protein, which are consistent with the structural characteristics of AHSA1 protein family. This protein shows high structural similarities to the prokaryotic proteins RHE_CH02687 from Rhizobium etli and YndB from B acillus subtilis , which can bind with flavinoids. Unlike these two homologs, CHU_1110 shows no obvious interaction with flavonoids in NMR titration experiments. In addition, no direct interaction has been observed between CHU_1110 and ATP, although many homologous sequences of CHU_1110 have been annotated as ATPase. Combining the analysis of structural similarity of CHU_1110 and genomic context of its encoding gene, we speculate that CHU_1110 may be involved in the stress response of bacteria to heavy metal ions, even though its specific biological functions that need to be further investigated.