Biomedical subjects

Angshuman Bagchi

Publications and source records attributed to Angshuman Bagchi.

7 recordsLinked to original sources

PubMed2006

Structural study of two proteins SigE and ORF1 to predict their roles in the biochemical oxidation of sulfur anions via the global sulfur oxidation operon (sox).

Microbial redox reactions involving inorganic sulfur compounds in the environment are one of the major reactions of the global sulfur cycle. These reactions are mediated by phylogenetically diverse prokaryotes containing the sulfur oxidizing gene cluster (sox). The sox gene cluster of alpha-Proteobacteria comprises of at least 15 genes, which form two transcriptional units. Recently two new orfs, which code for proteins named, SigE and ORF1, were identified in Starkeya novella. Sequence analyses reveal that SigE protein has the signature sequence of ECF-type sigma factors and a helix-turn-helix (HTH) DNA binding motif whereas ORF1 is possibly an anti ECF-sigma factor, which also has the signature sequence of the dsr family of sulfate ion binding proteins. We employed homology modeling to construct the three-dimensional structures of these proteins. The model of SigE was docked on to its promoter DNA to investigate the favourable binding modes of the protein. Interactions of SigE with its anti-sigma factor ORF1 were also reported after docking these proteins. We also identified the putative sulfate ion binding residues of ORF1 by docking sulfate ion on to it. Our study provides a rational framework for understanding of the structural as well as the molecular basis of the mechanism of the regulation of sulfur oxidation reactions by SigE and ORF1 proteins via the sox operon.

Anions↗

PubMed2005

A structural study towards the understanding of the interactions of SoxY, SoxZ, and SoxB, leading to the oxidation of sulfur anions via the novel global sulfur oxidizing (sox) operon.

Microbial redox reactions of inorganic sulfur compounds, mainly the sulfur anions, are one of the vital reactions responsible for the environmental sulfur balance. These reactions are mediated by phylogenetically diverse prokaryotes, which also take part in the extraction of metal ions from their sulfur containing ores. The sulfur oxidizing gene cluster (sox) of alpha-Proteobacteria comprises of at least 16 genes, forming two transcriptional units, viz., soxSRT and soxVWXYZABCDEFGH. SoxY is known to be a sulfur covalently binding protein, which binds sulfur anions (such as sulfate) to form SoxY-thiocysteine-S-sulfate, the first covalently bound sulfur adduct in the novel global sulfur anion oxidation cycle. SoxZ, a sulfur compound chelating protein, binds to SoxY forming a complex to which SoxB, a sulfate thiol-esterase, binds and ultimately cleaves the sulfur adduct. We employed homology modeling to construct the three-dimensional structures of the SoxY, SoxZ, and SoxB from Paracoccus pantotrophus. With the help of docking and molecular dynamics studies we have identified the residues of SoxY, SoxZ, and SoxB involved in the interaction. The probable mechanisms of the binding of SoxY with sulfate as well as the removal of sulfate from the SoxYZ complex are also established. Our study provides a rational basis to illustrate the molecular mechanism of the biochemistry of sulfur anion oxidation reactions by these industrially important organisms.

Alphaproteobacteria↗

PubMed2005

Structural insight into the interactions of SoxV, SoxW and SoxS in the process of transport of reductants during sulfur oxidation by the novel global sulfur oxidation reaction cycle.

Microbial redox reactions involving inorganic sulfur compounds, mainly the sulfur anions, are one of the vital reactions responsible for the environmental sulfur balance. These reactions are mediated by phylogenetically diverse prokaryotes, some of which also take part in the extraction of metal ions from their sulfur containing ores. These sulfur oxidizers oxidize inorganic sulfur compounds like sulfide, thiosulfate etc. to produce reductants that are used for carbon dioxide fixation or in respiratory electron transfer chains. The sulfur oxidizing gene cluster (sox) of alpha-Proteobacteria comprises of at least 15 genes, forming two transcriptional units, viz., soxSR and soxVWXYZABCDEFGH. SoxV is known to be a CcdA homolog involved in the transport of reductants from cytoplasm to periplasm. SoxW and SoxS are periplasmic thioredoxins, which (SoxW) interact with SoxV and thereby help in the redox reactions. We have employed homology modeling to construct the three-dimensional structures of the SoxV, SoxW and SoxS proteins from Rhodovulum sulfidophilum. With the help of docking and molecular dynamics simulations we have identified the amino acid residues of these proteins involved in the interaction. The probable biochemical mechanism of the transport of reductants through the interactions of these proteins has also been investigated. Our study provides a rational basis to interpret the molecular mechanism of the biochemistry of sulfur anion oxidation reactions by these ecologically important organisms.

Alphaproteobacteria↗

PubMed2005

Structural insight into SoxC and SoxD interaction and their role in electron transport process in the novel global sulfur cycle in Paracoccus pantotrophus.

Microbial oxidation of reduced inorganic sulfur compounds mainly sulfur anions in the environment is one of the major reactions of the global sulfur cycle mediated by phylogenetically diverse prokaryotes. The sulfur oxidizing gene cluster (sox) of alpha-Proteobacteria comprises of at least 16 genes, which form two transcriptional units, viz., soxSRT and soxVWXYZABCDEFGH. Sequence analysis reveals that soxD gene product (SoxD) belongs to the di-heme cytochrome c family of electron transport proteins whereas soxC gene product (SoxC) is a sulfur dehydrogenase. We employed homology modeling to construct the three-dimensional structures of the SoxC and SoxD from Paracoccus pantotrophus. SoxD protein is known to interact with SoxC. With the help of docking studies we have identified the residues involved in the interaction of SoxC and SoxD. The putative active site geometries of these two proteins as well as the structural basis of the involvements of these proteins in electron transport process during the oxidation of sulfur anions are also investigated.

Amino Acid Sequence↗

PubMed2005

Homology modeling of a transcriptional regulator SoxR of the Lithotrophic sulfur oxidation (Sox) operon in alpha-proteobacteria.

Microbial oxidation of reduced inorganic sulfur compounds in the environment is one of the major reactions of the global sulfur cycle mediated by phylogenetically diverse prokaryotes. The sulfur oxidizing gene cluster (sox) of alpha-Proteobacteria comprises of at least 15 genes, which form two transcriptional units, viz soxSRT and soxVWXYZABCDEFGH. Sequence analysis reveals that SoxR belongs to the ArsR family of helix-turn-helix DNA binding proteins. Although SoxR proteins do not contain the conserved metal-binding box, ELCVCDL, but there are a number of well conserved residues present throughout the sequence that are previously identified in the known ArsR family proteins. We employed homology modeling to construct the three-dimensional structure of the SoxR from chemolithotrophic alpha-Proteobacteria Pseudaminobacter salicylatoxidans KCT001. The predicted homology model of SoxR shows an overall structural similarity with winged helix-turn-helix family proteins. Since dimerization is essential for DNA binding and repression by the ArsR family proteins we have generated the dimeric model of SoxR that enables us to predict the DNA binding residues of the protein as well as the interaction of SoxR with the predicted promoter region of sox gene cluster.

Alphaproteobacteria↗

PubMed2005

Tetrathiobacter kashmirensis gen. nov., sp. nov., a novel mesophilic, neutrophilic, tetrathionate-oxidizing, facultatively chemolithotrophic betaproteobacterium isolated from soil from a temperate orchard in Jammu and Kashmir, India.

Twelve chemolithotrophic strains were isolated from temperate orchard soil on reduced sulfur compounds as energy and electron sources and characterized on the basis of their physiological properties and ability to oxidize various reduced sulfur compounds. The new isolates could oxidize tetrathionate as well as thiosulfate, and oxidation of the latter involved conversion of thiosulfate to tetrathionate followed by its accumulation and eventual oxidation to sulfate, manifested in the production of acid. The mesophilic, neutrophilic, Gram-negative and coccoid bacteria had a respiratory metabolism. Physiologically and biochemically, all the strains were more or less similar, differing only in their growth rates and ability to utilize a few carbon compounds as single heterotrophic substrates. 16S rRNA gene sequence analysis was performed with five representative strains, which revealed a high degree of similarity (> or =99%) among them and placed the cluster in the 'Betaproteobacteria'. The strains showed low levels (93.5-95.3 %) of 16S rRNA gene sequence similarity to Pigmentiphaga kullae, Achromobacter xylosoxidans, Pelistega europaea and species belonging to the genera Alcaligenes, Taylorella and Bordetella. The taxonomic coherence of the new isolates was confirmed by DNA-DNA hybridization. On the basis of their uniformly low 16S rRNA gene sequence similarities to species of all the closest genera, unique fatty acid profile, distinct G+C content (54-55.2 mol%) and phenotypic characteristics that include efficient chemolithotrophic utilization of tetrathionate, the organisms were classified in a new genus, Tetrathiobacter gen. nov. In the absence of any significant discriminatory phenotypic or genotypic characteristics, all the new isolates are considered to constitute a single species, for which the name Tetrathiobacter kashmirensis sp. nov. (type strain WT001(T)=LMG 22695(T)=MTCC 7002(T)) is proposed.

Bacterial Typing Techniques↗

PubMed2005

Active site driven ligand design: an evolutionary approach.

An evolutionary approach for designing a ligand molecule that can bind to the active site of a target protein is described in this article. An earlier attempt in this regard assumed a fixed tree structure of the ligand on both sides of the pharmacophore, and used a genetic algorithm for optimizing the van der Waals energy. However, it is evident that knowledge about the size of the tree is difficult to obtain an a priori. Moreover, it will also change from one active site to another. This limitation is overcome in the present article by using variable string length genetic algorithm (VGA) for evolving an appropriate arrangement of the basic functional units of the molecule to be designed, whose size may now vary. The crossover and mutation operators are appropriately redesigned in order to tackle the concept of variable length chromosomes. Once the geometry of the molecule is obtained, the possible three-dimensional structure and its docking energy is determined. Results are demonstrated for five different target proteins both numerically and pictorially. It is found that not only does the molecule designed using variable length representation, in general, have lower energy values, the docking energies are also lower, as compared to the molecule evolved using fixed size representation.

Binding Sites↗