5Y9S

Crystal structure of VV2_1132, a LysR family transcriptional regulator

Summary for 5Y9S

• Entry DOI: 10.2210/pdb5y9s/pdb
• Descriptor: VV2_1132, BROMIDE ION (3 entities in total)
• Functional Keywords: lysr, transcription
• Biological source: Vibrio vulnificus CMCP6
• Total number of polymer chains: 4
• Total formula weight: 138125.64

Authors

Jang, Y.,Hong, S.,Jo, I.,Ahn, J.,Ha, N.C. (deposition date: 2017-08-28, release date: 2018-03-28, Last modification date: 2024-03-27)

Primary citation

Jang, Y.,Choi, G.,Hong, S.,Jo, I.,Ahn, J.,Choi, S.H.,Ha, N.C.
A Novel Tetrameric Assembly Configuration in VV2_1132, a LysR-Type Transcriptional Regulator inVibrio vulnificus
Mol. Cells, 41:301-310, 2018

PubMed Abstract: LysR-type transcriptional regulators (LTTRs) contain an N-terminal DNA binding domain (DBD) and a C-terminal regulatory domain (RD). Typically, LTTRs function as homotetramers. VV2_1132 was identified in as an LTTR that is a homologue of HypT (also known as YjiE or QseD) in . In this study, we determined the crystal structure of full-length VV2_1132 at a resolution of 2.2 Å, 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 HypT, indicating that further study is required to elucidate the function of this gene in . The unique structure of VV2_1132 extends our knowledge of LTTR function and mechanisms of action.

PubMed: 29487273
DOI: 10.14348/molcells.2018.2190

Experimental method

X-RAY DIFFRACTION (2.199 Å)