9BCE

Shewanella oneidensis LysR family regulator SO0839 regulatory domain

Summary for 9BCE

• Entry DOI: 10.2210/pdb9bce/pdb
• Descriptor: Transcriptional regulator LysR family (2 entities in total)
• Functional Keywords: regulator, acetyl-coa, carboxylase, transcription
• Biological source: Shewanella oneidensis
• Total number of polymer chains: 2
• Total formula weight: 47911.36

Authors

Han, S.R.,Liang, H.H.,Lin, Z.H.,Fan, Y.L.,Ye, K.,Gao, H.G.,Tao, Y.J.,Jin, M. (deposition date: 2024-04-08, release date: 2024-11-20, Last modification date: 2024-12-11)

Primary citation

Xu, Y.,Lin, Z.,Hou, J.,Ye, K.,Han, S.,Liang, Y.,Liang, H.,Wu, S.,Tao, Y.J.,Gao, H.
A bacterial transcription activator dedicated to the expression of the enzyme catalyzing the first committed step in fatty acid biosynthesis.
Nucleic Acids Res., 52:12930-12944, 2024

PubMed Abstract: Acetyl-CoA carboxylase (ACCase) catalyzes the first committed and rate-limiting step of de novo fatty acid synthesis (FAS). Although this step is tightly regulated, regulators that specifically control transcription of the ACCase genes remain elusive. In this study, we identified LysR-type transcriptional regulator AccR as a dedicated activator for the transcription of accS, a gene encoding a multiple-domain ACCase in Shewanella oneidensis. We showed that AccR interacts with the accS promoter in vivo in response to changes in acetyl-CoA levels and in vitro. Analysis of the crystal structure of the effector-binding domain (EBD) of AccR identified two potential ligand-binding pockets, one of which is likely to bind acetyl-CoA as a ligand based on results from molecular docking, direct binding assay and mutational analysis of the residues predicted to interact with acetyl-CoA. Despite this, the interaction between AccR and acetyl-CoA alone appears unstable, implying that an additional yet unknown ligand is required for activation of AccR. Furthermore, we showed that AccR is acetylated, but the modification may not be critical for sensing acetyl-CoA. Overall, our data substantiate the existence of a dedicated transcriptional regulator for ACCases, expanding our current understanding of the regulation of FAS.

PubMed: 39475184
DOI: 10.1093/nar/gkae960

Experimental method

X-RAY DIFFRACTION (1.4 Å)