期刊
FEBS LETTERS
卷 590, 期 20, 页码 3583-3594出版社
WILEY
DOI: 10.1002/1873-3468.12425
关键词
bacteria; crystal structure H-NS; nucleoid-associated protein; protein-protein interaction; Pseudomonas
资金
- Platform Project for Supporting in Drug Discovery and Life Science Research (Platform for Drug Discovery, Informatics, and Structural Life Science, PDIS) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Japan Agency for Medical Research and Development (AMED) [2023, 2053]
- Kato Memorial Bioscience Foundation
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.
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