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• W2521455967 abstract "H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB." @default.
• W2521455967 created "2016-09-30" @default.
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• W2521455967 date "2016-10-01" @default.
• W2521455967 modified "2023-10-03" @default.
• W2521455967 title "Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in<i>Pseudomonas putida</i>KT2440" @default.
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• W2521455967 doi "https://doi.org/10.1002/1873-3468.12425" @default.
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