Crystallization and Preliminary X-ray Diffraction Analysis of the ArsC Protein from the Escherichia coli Arsenical Resistance Plasmid, R773

Mel, V. Srini J. De; Doyle, M. A.; Gladysheva, Tatiana; Oden, Kristine L.; Martin, Philip D.; Rosen, Barry P.; Edwards, Brian F.P.

doi:10.1006/jmbi.1994.1618

Cited by 3 publications

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“…that reduce Cr(VI) are P. ambigua C-13 and P.¯uorescens LB300, the latter aerobically and anaerobically (Bopp and Ehrlich, 1988). Among enterobacterial strains, Enterobacter aerogenes EAO reduced Cr(VI) in rich medium, with chromate reductase activity induced by nitrite (Clark, 1994), whereas E. cloacae HO1 reduced up to 2 mM CrO 4 2) to Cr(III), which was precipitated in the culture medium as Cr(OH) 3 anaerobically (Komori et al, 1990) at pH 7.0 to 7.8 (De Mel et al, 1994). In contrast, Escherichia coli ATCC 33456 reduced Cr(VI) aerobically and anaerobically within 12 h (Shen and Wang, 1993), but the product of the reaction [probably Cr(III)] was almost completely (98%) retained in a soluble form in the culture supernatant (Shen and Wang, 1993).…”

Section: Introductionmentioning

confidence: 99%

Effect of complexing agents on reduction of Cr(VI) by Desulfovibrio vulgaris ATCC 29579

Mabbett

Lloyd

Macaskie

2002

Biotech & Bioengineering

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The reduction of Cr(VI) at the expense of molecular hydrogen was studied using resting cells of Desulfovibrio vulgaris ATCC 29579 in anaerobic resting cell suspensions in MOPS buffer. Bioreduction occurred only in the presence of ligands or chelating agents (CO32-, citrate, NTA, EDTA, DTPA). The stimulatory effect of these ligands on the rate of Cr(VI) reduction was correlated (r = 0.988) with the strength of the ligand/chelate complex of Cr(III). The data are examined with respect to likely solution and redox equilibria in the ionic matrix of the carrier solution, and with respect to the potential for bioremediation of Cr(VI).

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Section: Introductionmentioning

confidence: 99%

Effect of complexing agents on reduction of Cr(VI) by Desulfovibrio vulgaris ATCC 29579

Mabbett

Lloyd

Macaskie

2002

Biotech & Bioengineering

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Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases

Bennett

Guan

Laurberg

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

129

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Arsenate is an abundant oxyanion that, because of its ability to mimic the phosphate group, is toxic to cells. Arsenate reductase (EC 1.97.1.5; encoded by the arsC gene in bacteria) participates to achieve arsenate resistance in both prokaryotes and yeast by reducing arsenate to arsenite; the arsenite is then exported by a specific transporter. The crystal structure of Bacillus subtilis arsenate reductase in the reduced form with a bound sulfate ion in its active site is solved at 1.6-Å resolution. Significant structural similarity is seen between arsenate reductase and bovine low molecular weight protein tyrosine phosphatase, despite very low sequence identity. The similarity is especially high between their active sites. It is further confirmed that this structural homology is relevant functionally by showing the phosphatase activity of the arsenate reductase in vitro. Thus, we can understand the arsenate reduction in the light of low molecular weight protein tyrosine phosphatase mechanism and also explain the catalytic roles of essential residues such as Cys-10, Cys-82, Cys-89, Arg-16, and Asp-105. A ''triple cysteine redox relay'' is proposed for the arsenate reduction mechanism.

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Preparation and crystallization of aBacillus subtilisarsenate reductase

Guan¹,

Hederstedt²,

Li³

et al. 2001

Acta Crystallogr D Biol Cryst

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Arsenate reductase (AR) in B. subtilis is encoded by the chromosomal arsC gene. Together with arsB and arsR, arsC participates in detoxification processes for the arsenate and arsenite ions. Full-length arsenate reductase without any modification has been expressed in Escherichia coli and purified in a soluble form. The recombinant protein has been crystallized at 277 K using polyethyleneglycol (PEG) or poly(ethyleneglycol) methyl ether (PME) as the main precipitant. At least two forms of crystals large enough for data collection have been obtained from wild-type protein under different conditions. An orthorhombic crystal diffracted to beyond 2.2 A with space group P2(1)2(1)2(1) and unit-cell parameters a = 51.22, b = 91.62, c = 101.93 A. A near-complete data set has been collected to 2.5 A. The application of the flash-annealing technique was crucial for high resolution during the data collection. The SeMet-substituted AR has also been produced and crystallized under very similar conditions as the wild type, but the unit-cell parameters are very different. The crystals of the SeMet protein diffracted to higher resolution than those of the wild type.

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Crystallization and Preliminary X-ray Diffraction Analysis of the ArsC Protein from the Escherichia coli Arsenical Resistance Plasmid, R773

Cited by 3 publications

References 0 publications

Effect of complexing agents on reduction of Cr(VI) by Desulfovibrio vulgaris ATCC 29579

Effect of complexing agents on reduction of Cr(VI) by Desulfovibrio vulgaris ATCC 29579

Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases

Preparation and crystallization of aBacillus subtilisarsenate reductase

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