Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from<i>Escherichia coli</i>

Hou, Yanjie; Li, De Feng; Wang, Da Cheng

doi:10.1107/s1744309113011937

Cited by 7 publications

(5 citation statements)

References 24 publications

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“…2B). PDE domain dimers have been previously identified (Table S2) [15–17,19,37,38]. PDE dimerisation involving PDE‐α6 and the R helix has implications for active site formation.…”

Section: Resultsmentioning

confidence: 99%

Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi‐functional c‐di‐GMP regulator

et al. 2014

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a b s t r a c tDiguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively synthesise and hydrolyse the secondary messenger cyclic dimeric GMP (c-di-GMP), and both activities are often found in a single protein. Intracellular c-di-GMP levels in turn regulate bacterial motility, virulence and biofilm formation. We report the first structure of a tandem DGC-PDE fragment, in which the catalytic domains are shown to be active. Two phosphodiesterase states are distinguished by active site formation. The structures, in the presence or absence of c-di-GMP, suggest that dimerisation and binding pocket formation are linked, with dimerisation being required for catalytic activity. An understanding of PDE activation is important, as biofilm dispersal via c-di-GMP hydrolysis has therapeutic effects on chronic infections.

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“…2B). PDE domain dimers have been previously identified (Table S2) [15–17,19,37,38]. PDE dimerisation involving PDE‐α6 and the R helix has implications for active site formation.…”

Section: Resultsmentioning

confidence: 99%

Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi‐functional c‐di‐GMP regulator

et al. 2014

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“…Recent studies identifying direct interactions between diguanylate cyclases and motility machinery − suggested that Pcc GCS regulation of O 2 -dependent motility could be due to protein–protein interactions with motility-related proteins in the same operon. Therefore, interactions between Pcc GCS and other P. carotovorum proteins were identified by affinity pull-down assays followed by mass spectrometry analysis.…”

Section: Resultsmentioning

confidence: 99%

Oxygen-Dependent Globin Coupled Sensor Signaling Modulates Motility and Virulence of the Plant Pathogen Pectobacterium carotovorum

et al. 2017

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Bacterial pathogens utilize numerous signals to identify the presence of their host and coordinate changes in gene expression that allow for infection. Within plant pathogens, these signals typically include small molecules and/or proteins from their plant hosts and bacterial quorum sensing molecules to ensure sufficient bacterial cell density for successful infection. In addition, bacteria use environmental signals to identify conditions when the host defenses are weakened and potentially to signal entry into an appropriate host/niche for infection. A globin coupled sensor protein (GCS), termed PccGCS, within the soft rot bacterium Pectobacterium carotovorum ssp. carotovorum WPP14 has been identified as an O sensor and demonstrated to alter virulence factor excretion and control motility, with deletion of PccGCS resulting in decreased rotting of a potato host. Using small molecules that modulate bacterial growth and quorum sensing, PccGCS signaling also has been shown to modulate quorum sensing pathways, resulting in the PccGCS deletion strain being more sensitive to plant-derived phenolic acids, which can function as quorum sensing inhibitors, and exhibiting increased N-acylhomoserine lactone (AHL) production. These findings highlight a role for GCS proteins in controlling key O-dependent phenotypes of pathogenic bacteria and suggest that modulating GCS signaling to limit P. carotovorum motility may provide a means to decrease rotting of plant hosts.

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“…C-di-GMP regulates swimming motility through a transcription factor FleQ which actives the transcription of genes involved in the biosynthesis of flagellum (Baraquet and Harwood, 2013). C-di-GMP can also directly bind with YcgR, which functions as a brake of flagellum to inhibit the rotation of flagellum (Paul et al, 2010) (Hou et al, 2013). A recent report has shown that c-di-GMP can also bind with ATPase FliI, a component of flagellar export apparatus (Trampari et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa

Zhu

Liu

et al. 2016

Environmental Microbiology

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Cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa, an opportunistic pathogen that can cause diverse infections. Here we report the crystal structure of GGDEF domain from SadC and the critical role of the trans-membrane (TM) domain of SadC with regard to biofilm formation, exopolysaccharide production and motility. We showed that over-expression of SadC in P. aeruginosa PAO1 totally inhibited swimming motility and significantly enhanced the production of exopolysaccharide Psl. SadC lacking TM domains (SadC ) could not localize on cytoplasmic membrane and form cluster, lost the ability to inhibit the swimming and twitching motility, and showed the attenuated activity to promote Psl production despite that SadC was able to catalyze the synthesize of c-di-GMP in vitro and in vivo. The GGDEF domain of SadC has a typical GGDEF structure and the α-helix connected the TM domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Our data imply that membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers.

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Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP fromEscherichia coli

Cited by 7 publications

References 24 publications

Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi‐functional c‐di‐GMP regulator

Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi‐functional c‐di‐GMP regulator

Oxygen-Dependent Globin Coupled Sensor Signaling Modulates Motility and Virulence of the Plant Pathogen Pectobacterium carotovorum

Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa

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