The TP0796 Lipoprotein of Treponema pallidum Is a Bimetal-dependent FAD Pyrophosphatase with a Potential Role in Flavin Homeostasis

Deka, Ranjit K.; Brautigam, Chad A.; Liu, Wei Z.; Tomchick, Diana R.; Norgard, Michael V.

doi:10.1074/jbc.m113.449975

Cited by 24 publications

(105 citation statements)

References 80 publications

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“…When our manuscript was under revision, a paper by Deka et al (52) appeared online on an ApbE-like protein from T. pallidum, reporting that this protein catalyzes a "single-turnover" hydrolysis of FAD to yield FMN and AMP. Although such an unusual activity is feasible as a side reaction of flavin transfer, we could not detect it with V. cholerae ApbE.…”

Section: Discussionmentioning

confidence: 99%

Alternative Pyrimidine Biosynthesis Protein ApbE Is a Flavin Transferase Catalyzing Covalent Attachment of FMN to a Threonine Residue in Bacterial Flavoproteins

Bertsova

Fadeeva

Kostyrko

et al. 2013

Journal of Biological Chemistry

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Background:The ApbE protein with unknown function is widespread in bacteria. Results: ApbE catalyzes Mg 2ϩ -dependent FMN transfer from FAD to Thr residues of flavoproteins in vitro and in vivo. Conclusion: ApbE is a novel modifying enzyme involved in the maturation of flavoproteins. Significance: Broad distribution of ApbE suggests a wide utilization of flavoproteins containing FMN attached via a phosphoester bond.

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Section: Discussionmentioning

confidence: 99%

Alternative Pyrimidine Biosynthesis Protein ApbE Is a Flavin Transferase Catalyzing Covalent Attachment of FMN to a Threonine Residue in Bacterial Flavoproteins

Bertsova

Fadeeva

Kostyrko

et al. 2013

Journal of Biological Chemistry

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“…Another lipoprotein, TP0655, was shown to be the SBP for a polyamine transporter (PotABCD (TP0652-0655)) with nanomolar binding affinities for putrescine and spermidine 99 . The X-ray structure of TP0298, also a lipoprotein, revealed it to be the SBP of a riboflavin transporter (RfuABCD (TP0298-0302)) 41 which collaborates with a dual function FAD pyrophosphatase-FMN transferase (Ftp (TP0796)) 42,100 to meet the T. pallidum ’s prodigious requirements for flavin cofactors. A longstanding question has been how T. pallidum , a fatty acid auxotroph, obtains essential long-chain fatty acids (LCFAs).…”

Section: What Lays Beneathmentioning

confidence: 99%

Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen

et al. 2016

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The last two decades have seen a worldwide resurgence in infections caused by Treponema pallidum subsp. pallidum, the syphilis spirochete. The syphilis spirochete’s well-recognized capacity for early dissemination and immune evasion has earned it the designation ‘the stealth pathogen’. Despite the many hurdles to studying syphilis pathogenesis, most notably the inability to culture and to genetically manipulate T. pallidum, in recent years, considerable progress has been made in elucidating the structural, physiologic, and regulatory facets of stealth pathogenicity. In this Review, we integrate this eclectic body of information to garner fresh insights into the highly successful parasitic lifestyles of the syphilis spirochete and related pathogenic treponemes.

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“…Because T. pallidum cannot be continuously cultivated in vitro , standard genetic approaches cannot be used to study the functions of its gene products. Accordingly, our efforts have focused on identifying undercharacterized periplasmic lipoproteins and attempting to garner functional information from their crystal structures …”

Section: Introductionmentioning

confidence: 99%

Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses

et al. 2014

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The sexually transmitted disease syphilis is caused by the bacterial spirochete Treponema pallidum. This microorganism is genetically intractable, accounting for the large number of putative and undercharacterized members of the pathogen's proteome. In an effort to ascribe a function(s) to the TP0435 (Tp17) lipoprotein, we engineered a soluble variant of the protein (rTP0435) and determined its crystal structure at a resolution of 2.42 Å . The structure is characterized by an eight-stranded b-barrel protein with a shallow "basin" at one end of the barrel and an ahelix stacked on the opposite end. Furthermore, there is a disulfide-linked dimer of the protein in the asymmetric unit of the crystals. Solution hydrodynamic experiments established that purified rTP0435 is monomeric, but specifically forms the disulfide-stabilized dimer observed in the crystal structure. The data herein, when considered with previous work on TP0435, imply plausible roles for the protein in either ligand binding, treponemal membrane architecture, and/or pathogenesis.

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The TP0796 Lipoprotein of Treponema pallidum Is a Bimetal-dependent FAD Pyrophosphatase with a Potential Role in Flavin Homeostasis

Cited by 24 publications

References 80 publications

Alternative Pyrimidine Biosynthesis Protein ApbE Is a Flavin Transferase Catalyzing Covalent Attachment of FMN to a Threonine Residue in Bacterial Flavoproteins

Alternative Pyrimidine Biosynthesis Protein ApbE Is a Flavin Transferase Catalyzing Covalent Attachment of FMN to a Threonine Residue in Bacterial Flavoproteins

Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen

Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses

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