Structural highlights
Publication Abstract from PubMed
LysR-type transcriptional regulators (LTTRs) contain an Nterminal DNA binding domain (DBD) and a C-terminal regulatory domain (RD). Typically, LTTRs function as homotetramers. VV2_1132 was identified in Vibrio vulnificus as an LTTR that is a homologue of HypT (also known as YjiE or QseD) in Escherichia coli. In this study, we determined the crystal structure of full-length VV2_1132 at a resolution of 2.2 A, thereby revealing a novel combination of the domains in the tetrameric assembly. Only one DBD dimer in the tetramer can bind to DNA, because the DNA binding motifs of the other DBD dimer are completely buried in the tetrameric assembly. Structural and functional analyses of VV2_1132 suggest that it might not perform the same role as E. coli HypT, indicating that further study is required to elucidate the function of this gene in V. vulnificus. The unique structure of VV2_1132 extends our knowledge of LTTR function and mechanisms of action.
A Novel Tetrameric Assembly Configuration in VV2_1132, a LysR-Type Transcriptional Regulator in Vibrio vulnificus.,Jang Y, Choi G, Hong S, Jo I, Ahn J, Choi SH, Ha NC Mol Cells. 2018 Feb 27. pii: molcells.2018.2190. doi:, 10.14348/molcells.2018.2190. PMID:29487273[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jang Y, Choi G, Hong S, Jo I, Ahn J, Choi SH, Ha NC. A Novel Tetrameric Assembly Configuration in VV2_1132, a LysR-Type Transcriptional Regulator in Vibrio vulnificus. Mol Cells. 2018 Feb 27. pii: molcells.2018.2190. doi:, 10.14348/molcells.2018.2190. PMID:29487273 doi:http://dx.doi.org/10.14348/molcells.2018.2190
