Crystal structure of Tflp: A ferredoxin‐like metallo‐β‐lactamase superfamily protein from <i>Thermoanaerobacter tengcongensis</i>

Gu, Shenyan; Yan, Xiaozhi; Liang, Dongcai

doi:10.1002/prot.22069

Cited by 5 publications

(7 citation statements)

References 25 publications

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“…An additional intense band at 320 nm is observed in the differential spectrum (Figure 4A), which can be assigned to a (Cys)S-Fe II LMCT [38]. Similar UV-vis specta were obtained for Tflp, a ferredoxin-like protein from Thermoanaerobacter tengcongensis [39] belonging to the metallo-β-lactamase superfamily, where a disulfide bond is near the di-Fe center in the active site.…”

Section: Resultsmentioning

confidence: 55%

Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

Campos-Bermudez¹,

Morán-Barrio²,

Costa-Filho³

et al. 2010

Journal of Inorganic Biochemistry

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Glyoxalase II (GLX2, EC 3.1.2.6., hydroxyacylglutathione hydrolase) is a metalloenzyme involved in crucial detoxification pathways. Different studies have failed in identifying the native metal ion of this enzyme, which is expressed with iron, zinc and/or manganese. Here we report that GloB, the GLX2 from Salmonella typhimurium, is differentially inhibited by glutathione (a reaction product) depending on the bound metal ion, and we provide a structural model for this inhibition mode. This metal-dependent inhibition was shown to occur in metal-enriched forms of the enzyme, complementing the spectroscopic data. Based on the high levels of free glutathione in the cell, we suggest that the expression of the different metal forms of GLX2 during Salmonella infection could be exploited as a mechanism to regulate the enzyme activity.

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Section: Resultsmentioning

confidence: 55%

Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

Campos-Bermudez¹,

Morán-Barrio²,

Costa-Filho³

et al. 2010

Journal of Inorganic Biochemistry

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“…Cellular oxidoreductases catalyze redox processes by transferring electrons from a reductant to oxidant and are important for protection against oxidative stress (Bisogno et al, 2010). The ferredoxin-like protein (FdxB) and iron transport protein HmuS are ubiquitous electron transfer proteins participating in the iron-sulfur cluster biosynthesis and a wide variety of redox reactions (Chao et al, 2005;Gu et al, 2008). In Rhizobium, the peroxidases and the catalases KatG (catalase HPI), KatE (catalase), and OhrB (organic hydroperoxide resistance) were known to participate in the antioxidant defense mechanism against H 2 O 2 -induced stress (Vargas Mdel et al, 2003), and the two electron transfer proteins FdxB and HmuS are also involved in a wide variety of redox reactions (Chao et al, 2005;Gu et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

Zou

Luo

et al. 2020

Front. Microbiol.

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GmcA is a FAD-containing enzyme belonging to the GMC (glucose-methanol-choline oxidase) family of oxidoreductases. A mutation in the Rhizobium leguminosarum gmcA gene was generated by homologous recombination. The mutation in gmcA did not affect the growth of R. leguminosarum, but it displayed decreased antioxidative capacity at H 2 O 2 conditions higher than 5 mM. The gmcA mutant strain displayed no difference of glutathione reductase activity, but significantly lower level of the glutathione peroxidase activity than the wild type. Although the gmcA mutant was able to induce the formation of nodules, the symbiotic ability was severely impaired, which led to an abnormal nodulation phenotype coupled to a 30% reduction in the nitrogen fixation capacity. The observation on ultrastructure of 4-week pea nodules showed that the mutant bacteroids tended to start senescence earlier and accumulate poly-β-hydroxybutyrate (PHB) granules. In addition, the gmcA mutant was severely impaired in rhizosphere colonization. Real-time quantitative PCR showed that the gmcA gene expression was significantly up-regulated in all the detected stages of nodule development, and statistically significant decreases in the expression of the redoxin genes katG, katE, and ohrB were found in gmcA mutant bacteroids. LC-MS/MS analysis quantitative proteomics techniques were employed to compare differential gmcA mutant root bacteroids in response to the wild type infection. Sixty differentially expressed proteins were identified including 33 up-regulated and 27 down-regulated proteins. By sorting the identified proteins according to metabolic function, 15 proteins were transporter protein, 12 proteins were related to stress response and virulence, and 9 proteins were related to transcription factor activity. Moreover, nine proteins related to amino acid metabolism were over-expressed.

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“…5a, 5b and 5c). No report is available on Tm1679, while a study on Tflp has been published in which Tflp was just described as a ferredoxin-like protein (Gu et al, 2008). The metal-coordination chemistry of Tflp is almost the same as that of TW9814 (Figs.…”

Section: Hypothetical Proteins Resembling Tw9814 In the Mbl Superfamilymentioning

confidence: 99%

“…The diffraction data were collected to a maximum resolution of 2.34 A ˚. The initial phases of TW9814 were determined by molecular replacement using a metallo--lactamase superfamily protein from Thermoanaerobacter tengcongensis (PDB entry 2p4z; Gu et al, 2008), which is the most structurally similar protein to TW9814. The final structural coordinates of TW9814 have been deposited with PDB code 7dck.…”

Section: Crystallization Data Collection and Structure Determinationmentioning

confidence: 99%

Structural and functional identification of the uncharacterized metallo-β-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination

Heo¹,

Park²,

Jeon³

et al. 2022

Acta Cryst Sect D Struct Biol

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Metallo-β-lactamase (MBL) superfamily proteins have a common αβ/βα sandwich fold and perform a variety of functions through metal-mediated catalysis. However, because of the enormous scale of this superfamily, only a small percentage of the proteins belonging to the superfamily have been annotated structurally or functionally to date. Therefore, much remains unknown about the MBL superfamily proteins. Here, TW9814, a hypothetical MBL superfamily protein, was structurally and functionally investigated. Guided by the crystal structure of dimeric TW9814, it was demonstrated that TW9814 functions as a phosphodiesterase (PDE) in the presence of divalent metal ions such as manganese(II) or nickel(II). A docking model between TW9814 and the substrate bis(p-nitrophenyl)phosphate (bpNPP) showed the importance of the dimerization of TW9814 for its bpNPP-hydrolyzing activity and for the interaction between the enzyme and the substrate. TW9814 showed outstanding catalytic efficiency (k cat/K m) under alkaline conditions compared with other PDEs. The activity of TW9814 appears to be regulated through a disulfide bond, which is a feature that is not present in other MBL superfamily members. This study provides a platform for the functional characterization of other hypothetical proteins of the MBL or other superfamilies.

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Crystal structure of Tflp: A ferredoxin‐like metallo‐β‐lactamase superfamily protein from Thermoanaerobacter tengcongensis

Cited by 5 publications

References 25 publications

Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

Structural and functional identification of the uncharacterized metallo-β-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination

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