alexa Abstract | In silico analysis of arsenate reductase from Enterobacter cloacae BC2 as a potential microorganism for reducing arsenate

Journal of Chemical and Pharmaceutical Research
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Arsenic is a toxic element present in the environme nt that causes serious health issues. Bacteria and higher organisms have developed resistance mechanisms to m ake arsenic harmless. The identification of arsenat e reductase (ArsC) in Escherichia coli is considered to be remarkable evidence for arsenic bioremediatio n. ArsC is an arsenic binding protein plays significant role in r eduction of arsenate to arsenite. The study is aime d to predict the structure and function of target ArsC protein of En terobacter cloacae using computational approaches a nd analyze the docking of arsenate to active arsenic binding s ites in modelled ArsC structure. The arsC gene from Enterobacter cloacae was identified, sequenced and submitted in NCBI Genbank database and its corresponding protein sequence was used for analysis. The prediction of p hysico-chemical properties such as isoelectric poin t (pI), molecular weight, number of atoms present, aliphati c index and grand average of hydropathicity (GRAVY) was carried out for protein sequence of ArsC using the EXPASY ProtParam server. Homology modeling of targe t ArsC protein was performed using EXPASY Swiss Model Work space and the structure was validated with Ramachan dran plot analysis using RAMPAGE tool. The two dimension al structure of arsenate ion is obtained from PUBCH EM database and converted to three dimensional (3D) fo rmat using online molecular converter tool. The doc king analysis of 3D structures of arsenate reductase pro tein and arsenate ion was carried out in PATCHDOCK server. The comparative analysis of physicochemical paramet ers reveals the functional similarity of ArsC prote in in both Enterobacter cloacae and E.coli. In the predicted h omology structure, 99% of amino acid residues lied in favourable region of Ramachandran plot, which confi rms ArsC structure of Enterobacter cloacae was ener getically stable. The docking of arsenate to active arsenic b inding sites in modelled structure was similar to a rsenic binding sites of E.coli ArsC. This study concludes that Ars C protein of Enterobacter cloacae structurally and functionally similar to ArsC of E.coli. Further ArsC from Entero bacter cloacae BC2 can play a significant role duri ng arsenic resistance and also act as potential microorganism for bioremediation of arsenic toxicity.

Author(s): M S Selvi P Chandra Sekar S Yuvaraj Abishek Albert Eldho Paul S Sasikumar and G S Selvam


Enterobacter cloacae, Escherichia coli, Arsenate reductase, Arsenic toxicity, arsenic resistance, Bioremediation., arsenate reductase, Enterobacter cloacae BC2

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