7CDX

Complex STRUCTURE OF A NOVEL VIRULENCE REGULATION FACTOR SghR with its effector sucrose

Summary for 7CDX

• Entry DOI: 10.2210/pdb7cdx/pdb
• Related PRD ID: PRD_900003
• Descriptor: LacI-type transcription factor, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: agrobacterium infection; plant-microbe interaction; laci rep sucrose, transcription
• Biological source: Agrobacterium tumefaciens A6
• Total number of polymer chains: 2
• Total formula weight: 82237.39

Authors

Ye, F.Z.,Wang, C.,Yan, X.F.,Zhang, L.H.,Gao, Y.G. (deposition date: 2020-06-20, release date: 2020-07-15, Last modification date: 2023-11-29)

Primary citation

Ye, F.,Wang, C.,Fu, Q.,Yan, X.F.,Bharath, S.R.,Casanas, A.,Wang, M.,Song, H.,Zhang, L.H.,Gao, Y.G.
Structural basis of a novel repressor, SghR, controllingAgrobacteriuminfection by cross-talking to plants.
J.Biol.Chem., 295:12290-12304, 2020

PubMed Abstract: infects various plants and causes crown gall diseases involving temporal expression of virulence factors. SghA is a newly identified virulence factor enzymatically releasing salicylic acid from its glucoside conjugate and controlling plant tumor development. Here, we report the structural basis of SghR, a LacI-type transcription factor highly conserved in family, regulating the expression of SghA and involved in tumorigenesis. We identified and characterized the binding site of SghR on the promoter region of and then determined the crystal structures of apo-SghR, SghR complexed with its operator DNA, and ligand sucrose, respectively. These results provide detailed insights into how SghR recognizes its cognate DNA and shed a mechanistic light on how sucrose attenuates the affinity of SghR with DNA to modulate the expression of SghA. Given the important role of SghR in mediating the signaling cross-talk during infection, our results pave the way for structure-based inducer analog design, which has potential applications for agricultural industry.

PubMed: 32651231
DOI: 10.1074/jbc.RA120.012908

Experimental method

X-RAY DIFFRACTION (2.103 Å)