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

Bennett, Matthew; Guan, Zhi; Laurberg, Martin; Su, Xiao‐Dong

doi:10.1073/pnas.241397198

Cited by 85 publications

(136 citation statements)

References 39 publications

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“…The crystal structure of reduced ArsC has been reported (Protein Data Bank code 1JL3) and contains four chains (chains A-D) in an asymmetric unit (22). Residues 3-139 can be seen in chains A and B and are in good agreement with the solution structure of reduced ArsC.…”

Section: Solution Structures Of the Reduced And Oxidized Forms Of B supporting

confidence: 53%

“…The overall folds of the reduced and oxidized forms of ArsC are very similar, containing a single ␣/␤-domain and showing a typical proteintyrosine phosphatase I-like fold (22). The reduced form of ArsC consists of seven helices (residues 16 -27 (␣1), 46 -54 (␣2), 60 -62 (3 10 helix 1), 69 -72 (␣3), 83-88 (3 10 helix 2), 106 -108 (3 10 helix 3), and 113-137 (␣4)) and a four-stranded ␤-sheet (residues 4 -10 (␤1), 32-38 (␤2), 77-80 (␤3), and 97-100 (␤4)), which are packed into a single ␣/␤-domain containing a central four-stranded parallel open twisted ␤-sheet flanked by four ␣-helices (Fig.…”

Section: Solution Structures Of the Reduced And Oxidized Forms Of B mentioning

confidence: 99%

“…After increasing the concentration of DTT, the HSQC spectra showed a unique set of peaks corresponding to the pure reduced form of ArsC. Notably, the concentration of DDT used in the crystal preparation was approximately five times that of the enzyme (14,22). In addition, the region from Cys 82 to Val 96 is well defined in the NMR structure of oxidized ArsC.…”

Section: Solution Structures Of the Reduced And Oxidized Forms Of B mentioning

confidence: 99%

“…ArsC is subsequently regenerated by thioredoxin, which converts the enzyme into the reduced form (21). The arsC gene of the Gram-positive bacteria Bacillus subtilis is located in the SKIN element in the chromosome and shares 64% identity with S. aureus ArsC (7,22). The conserved CX 5 R anion-binding motif containing Cys 10 , known as the P-loop, is proposed to be the arsenate-binding site (23).…”

mentioning

confidence: 99%

“…The crystal structure of the reduced form of B. subtilis ArsC has been reported and contains four molecules (chains A-D) in an asymmetric unit (22). The segment Cys 82 -Val 96 is missing in two chains (chains C and D) of the crystal structure, indicating a mixture of different conformations.…”

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confidence: 99%

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Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis

Guo

Peng

et al. 2005

Journal of Biological Chemistry

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Arsenate reductase encoded by the chromosomal arsC gene in Bacillus subtilis catalyzes the intracellular reduction of arsenate to arsenite, which is then extruded from cells through an efficient and specific transport system. Herein, we present the solution structures and backbone dynamics of both the reduced and oxidized forms of arsenate reductase from B. subtilis. The overall structures of both forms are similar to those of bovine low molecular weight protein-tyrosine phosphatase and arsenate reductase from Staphylococcus aureus. However, several features of the tertiary structure and mobility are notably different between the reduced and oxidized forms of B. subtilis arsenate reductase, particularly in the P-loop region and the segment Cys 82 -Cys 89 . The backbone dynamics results demonstrated that the reduced form of arsenate reductase undergoes millisecond conformational changes in the functional P-loop and Cys 82 -Cys 89 , which may facilitate the formation of covalent intermediates and subsequent reduction of arsenate. In the oxidized form, Cys 82 -Cys 89 shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond time scales, which may facilitate the reduction of the oxidized enzyme by thioredoxin to regenerate the active enzyme. Overall, the internal dynamics and static structures of the enzyme provide insights into the molecular mechanism of arsenate reduction, especially the reversible conformational switch and changes in internal motions associated with the catalytic reaction.

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Section: Solution Structures Of the Reduced And Oxidized Forms Of B supporting

confidence: 53%

Section: Solution Structures Of the Reduced And Oxidized Forms Of B mentioning

confidence: 99%

Section: Solution Structures Of the Reduced And Oxidized Forms Of B mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis

Guo

Peng

et al. 2005

Journal of Biological Chemistry

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Arsenic Metabolism in Prokaryotic and Eukaryotic Microbes

Bhattacharjee

Rosen

Microbiology Monographs

144

123

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Microbial Interactions in the Arsenic Cycle: Adoptive Strategies and Applications in Environmental Management

Dhuldhaj

Yadav

Singh

et al. 2012

Reviews of Environmental Contamination and Toxicology Volume 224

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Arsenic (As) is a nonessential element that is often present in plants and in other organisms. However, it is one of the most hazardous of toxic elements globally. In many parts of the world, arsenic contamination in groundwater is a serious and continuing threat to human health. Microbes play an important role in regulating the environmental fate of arsenic. Different microbial processes influence the biogeochemical cycling of arsenic in ways that affect the accumulation of different arsenic species in various ecosystem compartments. For example, in soil, there are bacteria that methylate arsenite to trimethylarsine gas, thereby releasing arsenic to the atmosphere.In marine ecosystems, microbes exist that can convert inorganic arsenicals to organic arsenicals (e.g., di- and tri-methylated arsenic derivatives, arsenocholine,arsenobetaine, arsenosugars, arsenolipids). The organo arsenicals are further metabolized to complete the arsenic cycle.Microbes have developed various strategies that enable them to tolerate arsenic and to survive in arsenic-rich environments. Such strategies include As exclusion from cells by establishing permeability barrier, intra- and extracellular sequestration,active efflux pumps, enzymatic reduction, and reduction in the sensitivity of cellular targets. These strategies are used either singly or in combination. In bacteria,the genes for arsenic resistance/detoxification are encoded by the arsenic resistance operons (ars operon).In this review, we have addressed and emphasized the impact of different microbial processes (e.g., arsenite oxidation, cytoplasmic arsenate reduction, respiratory arsenate reduction, arsenite methylation) on the arsenic cycle. Microbes are the only life forms reported to exist in heavy arsenic-contaminated environments. Therefore,an understanding of the strategies adopted by microbes to cope with arsenic stress is important in managing such arsenic-contaminated sites. Further future insights into the different microbial genes/proteins that are involved in arsenic resistance may also be useful for developing arsenic resistant crop plants.

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

Cited by 85 publications

References 39 publications

Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis

Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis

Arsenic Metabolism in Prokaryotic and Eukaryotic Microbes

Microbial Interactions in the Arsenic Cycle: Adoptive Strategies and Applications in Environmental Management

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