The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families

Bordo, Domenico; Deriu, Daniela; Colnaghi, Rita; Carpen, Aristodemo; Pagani, Silvia; Bolognesi, Martino

doi:10.1006/jmbi.2000.3651

Cited by 84 publications

(106 citation statements)

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“…The ability of RhdA in maintaining A. vinelandii cellular redox status does imply that RhdA functions as a redox switch, a role that, in principle, might be accomplished by using as a player the highly reactive thiol of its catalytic cysteine residue (Bordo et al, 2000). The key role played by sulfhydryl groups (-SH) in the response to oxidative stress is emerging (Kiley and Storz, 2004;Poole et al, 2004;Jacob et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

“…PF00581; A. vinelandii DJ subgroup), thus making it conceivable that substrate recognition and biological interactions are driven by the specific active-site structures. The A. vinelandii tandem domain protein RhdA (Colnaghi et al, 1996) contains an active-site motif (HCQTHHR) not currently found in rhodanese-like proteins, that confers structural peculiarity of the environment of its catalytic cysteine residue (Bordo et al, 2000), the only one present in the molecule. RhdA, however, could represent a good model to prove a specific role of a rhodanese-like protein in the aerobe A. vinelandii.…”

Section: Introductionmentioning

confidence: 99%

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The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Remelli

Cereda

Papenbrock

et al. 2010

Biological Chemistry

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The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Remelli

Cereda

Papenbrock

et al. 2010

Biological Chemistry

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“…The closest homologs include bovine liver rhodanese ( Fig. 2B; Ploegman et al 1978a,b), Escherichia coli GlpE (Spallarossa et al 2001), Azotobacter vinelandii rhodanese (Bordo et al 2000), Leishmania major 3-mercaptopyruvate sulfurtransferase (Alphey et al 2003), Thermus thermophilus single-domain rhodanese (Hattori et al 2006), and Wolinella succinogenes polysulfide-sulfurtransferase (Lin et al 2004). Interestingly, Cdc25A, a dual specificity phosphatase that has an important role in cell cycle control, also has the same backbone fold ( Fig.…”

Section: Structure Of the Map Kinase Binding Domainmentioning

confidence: 99%

“…the BD cannot have the same catalytic activity. Several of the rhodaneses contain two structurally homologous domains, but only one of them is catalytically active (Ploegman et al 1978a,b;Bordo et al 2000;Alphey et al 2003). The equivalent residue in the inactive domain of these enzymes has also been mutated.…”

Section: Structure Of the Map Kinase Binding Domainmentioning

confidence: 99%

Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5

Tao

Tong

2007

Protein Science

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MAP kinase phosphatases (MKPs) have crucial roles in regulating the signaling activity of MAP kinases and are potential targets for drug discovery against human diseases. These enzymes contain a catalytic domain (CD) as well as a binding domain (BD) that help recognize the target MAP kinase. We report here the crystal structures at up to 2.2 Å resolution of the BD and CD of human MKP5 and compare them to the known structures from other MKPs. Dramatic structural differences are observed between the BD of MKP5 and that of MKP3 determined previously by NMR. In particular, the cluster of positively charged residues that is important for MAP kinase binding is located in completely different positions in the two structures, with a distance of 25 Å between them. Moreover, this cluster is a-helical in MKP5, while it forms a loop followed by a b-strand in MKP3. These large structural differences could be associated with the distinct substrate preferences of these phosphatases, but further studies are needed to confirm this. The CD of MKP5 is observed in an active conformation, and two loops in the active site have backbone shifts of up to 5 Å relative to the inactive CDs from other MKPs.

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“…Most sulfurtransferases have an N-terminal "structural" domain and a C-terminal domain containing the active site (1,16,17). The vertebrate rhodaneses have been extensively studied in attempts to understand the part played by the N-terminal structural domain in the correct folding and stability of the enzymes.…”

mentioning

confidence: 99%

3-Mercaptopyruvate Sulfurtransferase of LeishmaniaContains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism

Williams

Kelly

Mottram

et al. 2003

Journal of Biological Chemistry

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Cytosolic 3-mercaptopyruvate sulfurtransferases (EC 2.8.1.2) of Leishmania major and Leishmania mexicana have been cloned, expressed as active enzymes in Escherichia coli, and characterized. The leishmanial singlecopy genes predict a sulfurtransferase that is structurally peculiar in possessing a C-terminal domain of some 70 amino acids. Homologous genes of Trypanosoma cruzi and Trypanosoma brucei encode enzymes with a similar C-terminal domain, suggesting that this feature, not known in any other sulfurtransferase, is a characteristic of trypanosomatid parasites. Short truncations of the C-terminal domain resulted in misfolded inactive proteins, demonstrating that the domain plays some key role in facilitating correct folding of the enzymes. The leishmanial recombinant enzymes exhibited high activity toward 3-mercaptopyruvate and catalyzed the transfer of sulfane sulfur to cyanide to form thiocyanate. They also used thiosulfate as a substrate and reduced thioredoxin as the accepting nucleophile, the latter being oxidized. The enzymes were expressed in all life cycle stages, and the expression level was increased under peroxide or hypo-sulfur stress. The results are consistent with the enzymes having an involvement in the synthesis of sulfur amino acids per se or iron-sulfur centers of proteins and the parasite's management of oxidative stress.

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The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families

Cited by 84 publications

References 64 publications

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5

3-Mercaptopyruvate Sulfurtransferase of LeishmaniaContains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism

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