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ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13 and Cys Responses Submit a Letter to the Editor. Arsenic is a toxic metalloid found in water, soil, and air from both natural and anthropogenic sources.

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All spectra were fit using identical protocols, first by distinguishing the best single-shell fit to the data and then by progressively adding extra scattering environments to the fit. The publisher’s final edited version of this article is available at Biochemistry. Thus, the affinity of each of the three cysteine mutants decreased by fold or more compared with the parental protein containing Cys12, Cys13, and Cys Circular dichroism CD spectra from to nm were recorded with a spectrometer from Olis Inc.

The Se-Met crystals had three molecules in the asymmetric unit, and an initial model of of the total residues was automatically built with PHENIX.

Not only does ArsD fit well into the cavity of the open form of ArsA, but the residues of the two proteins that are proposed to interact exhibit reasonable complementarity. We also examined whether the same arsD mutants affected resistance conferred by the ArsAB pump.

ArsA exhibited an apparent affinity of 0. Most transition and heavy metal ions do not exist as free ions in the cytosol but are sequestered by a variety of proteins variously called metal ion chaperones, scaffolds, or intracellular carriers 4. The metalloid is a carcinogen and is considered a causative agent of a number of other diseases, including cardiovascular and neurological disorders 12.

It binds three ions with a conserved CC X C motif in which all three cysteines are required to produce active oxidase. Addition of GSH accelerated the rate by fold at pH 7.


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Ddiagrammatic representation of the ArsD monomer. Vogel G, Steinhart R. ArsA was added to a final concentration of 0. It should be pointed out that six-histidine tags do not bind As III Further experimental results will be necessary to test this proposed order of binding. Residues predicted to interact with ArsA are labeled. In these operons, an arsD gene is almost always adjacent to the arsA gene, suggesting a related function.

ArsD has two native tryptophan residues, Trp35 and Trp Protein expression levels were determined by immunoblotting using anti-ArsA and anti-ArsD antibodies. The costs of publication of this article were defrayed in part by the payment of page charges.

DNA Manipulations Plasmid extraction, DNA restriction endonuclease analysis, ligation, and other general molecular biological procedures were performed as described previously Health effects and risk assessment of arsenic.

ATPase activity was estimated using a coupled assay 22as described previously The data were integrated 1009 2 to 20 s in a k -weighted manner in the EXAFS region for a total scan length of 45 min. EXAFS fitting analysis was performed on raw unfiltered data.

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Here we report the structure of the arsenic metallochaperone ArsD at 1. In analogy with the agsd for the transfer of copper from chaperones to copper pumps or enzymes 9we previously proposed a stepwise transfer from the cysteines of ArsD to the cysteines of ArsA Binding of As III and ATP wrsd a series of conformational changes in ArsA, resulting in activation of catalysis, with final extrusion of the metalloid from the cells.

These results demonstrate that each MBS binds one atom of trivalent metalloid, for a total of three per monomer and six per dimer. X-ray energies were calibrated using an arsenic foil absorption spectrum collected simultaneously with the protein data. Considering that cysteine pair Cys 12 -Cys 13 arwd Cys 18 are conserved in all ArsD homologues identified to date, three derivatives were constructed: Health aesd associated with exposure to low levels of arsenite include cardiovascular and peripheral vascular disease, neurological disorders, diabetes mellitus, and various forms of cancer 12.


ClusPro is a ardd automated docking and discrimination server that filters docked conformations with good surface complementarity and ranks them based on their clustering properties. Based on this information, a model of the metallated form of the R ArsD Figure 4 was constructed taking into account the bond distances of 2.

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Reduction and binding of arsenate and dimethylarsinate by glutathione: The codons for residues Cys 12Cys 13Cys 18Cysand Cys in arsD 1— were changed individually or in pairs to alanines or deleted by the indicated truncations. Formation of fluorescent cross-linked products was visualized at nm and by immunoblotting with anti-serum against ArsD. Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray aarsd spectroscopy.

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Most of those had ArsD binding based on hydophobic-favored and van der Waals-favored coefficients to various locations on the surface of ArsA.

Glutathione biosynthesis in Escherichia coli K Hydrogen bonds and salt bridges are shown in dotted lines with distances.

Get the replacement part you need for your Hotpoint-Ariston Washing Machine from the UK’s largest supplier of appliance spare parts. Metal ion afsd function of the soluble Cu I receptor Atx1. Growth in liquid culture was estimated from the absorbance at nm. The final R cryst and R free values for ArsD were Since arad of As GS 3 is slow at pH 7. ClusPro Version 2, a web-based method accessible at http: Here the EXAFS data with wild-type ArsD unambiguously demonstrate that the binding site is a three-coordinate sulfur-containing site, similar in nature but not sequence to the ArsA As III binding site 35 and the three convergently evolved sites of three different ArsR repressors 2536 Ribbon diagram of the ArsD dimer showing the extensive interface between monomers.

Substitutions of the three cysteines in ArsD previously resulted in the loss of Sb III binding ability in gel filtration assays 6.