8K5Q

Crystal structure of YajQ STM0435 with c-di-GMP

Summary for 8K5Q

• Entry DOI: 10.2210/pdb8k5q/pdb
• Descriptor: YajQ, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (3 entities in total)
• Functional Keywords: structural genomics
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S
• Total number of polymer chains: 1
• Total formula weight: 19725.67

Authors

Dai, Y.,Zhang, M.,Wang, W.,Li, B. (deposition date: 2023-07-23, release date: 2024-04-17)

Primary citation

Dai , Y.,Liu , R.,Yue , Y.,Song , N.,Jia , H.,Ma , Z.,Gao , X.,Zhang , M.,Yuan , X.,Liu , Q.,Liu , X.,Li , B.,Wang , W.
A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella
Virulence, 15:2331265-, 2024

PubMed Abstract: Flagella play a crucial role in the invasion process of and function as a significant antigen that triggers host pyroptosis. Regulation of flagellar biogenesis is essential for both pathogenicity and immune escape of . We identified the conserved and unknown function protein STM0435 as a new flagellar regulator. The ∆ strain exhibited higher pathogenicity in both cellular and animal infection experiments than the wild-type . Proteomic and transcriptomic analyses demonstrated dramatic increases in almost all flagellar genes in the ∆ strain compared to wild-type . In a surface plasmon resonance assay, purified STM0435 protein-bound c-di-GMP had an affinity of ~8.383 µM. The crystal structures of apo-STM0435 and STM0435&c-di-GMP complex were determined. Structural analysis revealed that R33, R137, and D138 of STM0435 were essential for c-di-GMP binding. A with STM1987 (GGDEF protein) or STM4264 (EAL protein) overexpression exhibits completely different motility behaviours, indicating that the binding of c-di-GMP to STM0435 promotes its inhibitory effect on flagellar biogenesis.

PubMed: 38532247
DOI: 10.1080/21505594.2024.2331265

Experimental method

X-RAY DIFFRACTION (2.28 Å)