5b52

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b52 OCA], [https://pdbe.org/5b52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b52 RCSB], [https://www.ebi.ac.uk/pdbsum/5b52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b52 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440.,Suzuki-Minakuchi C, Kawazuma K, Matsuzawa J, Vasileva D, Fujimoto Z, Terada T, Okada K, Nojiri H FEBS Lett. 2016 Oct 6. doi: 10.1002/1873-3468.12425. PMID:27709616<ref>PMID:27709616</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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