5B52

Crystal structure of the N-terminal domain of H-NS family protein TurB

Summary for 5B52

• Entry DOI: 10.2210/pdb5b52/pdb
• Descriptor: H-NS family protein MvaT (2 entities in total)
• Functional Keywords: transcriptional regulator, nucleoid associated protein, transcription
• Biological source: Pseudomonas putida (strain KT2440)
• Total number of polymer chains: 2
• Total formula weight: 16008.58

Authors

Suzuki-Minakuchi, C.,Nojiri, H. (deposition date: 2016-04-21, release date: 2016-10-19, Last modification date: 2024-03-20)

Primary citation

Suzuki-Minakuchi, C.,Kawazuma, K.,Matsuzawa, J.,Vasileva, D.,Fujimoto, Z.,Terada, T.,Okada, K.,Nojiri, H.
Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440
Febs Lett., 590:3583-3594, 2016

PubMed 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.

PubMed: 27709616
DOI: 10.1002/1873-3468.12425

Experimental method

X-RAY DIFFRACTION (2.3 Å)