6JBX

Crystal structure of Streptococcus pneumoniae FabT in complex with DNA

Summary for 6JBX

• Entry DOI: 10.2210/pdb6jbx/pdb
• Descriptor: Fatty acid biosynthesis transcriptional regulator, DNA (5'-D(*AP*AP*TP*AP*GP*TP*TP*TP*GP*AP*CP*TP*GP*TP*CP*AP*AP*AP*TP*TP*AP*TP*G)-3'), DNA (5'-D(*CP*AP*TP*AP*AP*TP*TP*TP*GP*AP*CP*AP*GP*TP*CP*AP*AP*AP*CP*TP*AP*TP*T)-3'), ... (5 entities in total)
• Functional Keywords: transcription factor, marr family, fatty acid synthesis, transcription-dna complex, transcription/dna
• Biological source: Streptococcus pneumoniae; More
• Total number of polymer chains: 4
• Total formula weight: 50048.15

Authors

Zuo, G.,Chen, Z.P.,Li, Q.,Zhou, C.Z. (deposition date: 2019-01-27, release date: 2019-07-24, Last modification date: 2024-03-27)

Primary citation

Zuo, G.,Chen, Z.P.,Jiang, Y.L.,Zhu, Z.,Ding, C.,Zhang, Z.,Chen, Y.,Zhou, C.Z.,Li, Q.
Structural insights into repression of the Pneumococcal fatty acid synthesis pathway by repressor FabT and co-repressor acyl-ACP.
Febs Lett., 593:2730-2741, 2019

PubMed Abstract: The Streptococcus pneumoniae fatty acid synthesis (FAS) pathway is globally controlled at the transcriptional level by the repressor FabT and its co-repressor acyl carrier protein (acyl-ACP), the intermediate of phospholipid synthesis. Here, we report the crystal structure of FabT complexed with a 23-bp dsDNA, which indicates that FabT is a weak repressor with low DNA-binding affinity in the absence of acyl-ACP. Modification of ACP with a long-chain fatty acid is necessary for the formation of a stable complex with FabT, mimicked in vitro by cross-linking, which significantly elevates the DNA-binding affinity of FabT. Altogether, we propose a putative working model of gene repression under the double control of FabT and acyl-ACP, elucidating a distinct repression network for Pneumococcus to precisely coordinate FAS.

PubMed: 31291684
DOI: 10.1002/1873-3468.13534

Experimental method

X-RAY DIFFRACTION (2.2 Å)