In-Silico Structural and Functional Characterization of a V. cholerae O395 Hypothetical Protein Containing a PDZ1 and an Uncommon Protease Domain
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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| Title |
In-Silico Structural and Functional Characterization of a
V. cholerae O395 Hypothetical Protein Containing a PDZ1 and an Uncommon Protease Domain
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| Creator |
Dutta, Avirup
Katarkar, Atul Chaudhuri, Keya |
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| Subject |
Molecular & Human Genetics
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| Description |
Vibrio cholerae, the causative agent of epidemic cholera, has been a constant source of concern for decades. It has
constantly evolved itself in order to survive the changing environment. Acquisition of new genetic elements through
genomic islands has played a major role in its evolutionary process. In this present study a hypothetical protein was
identified which was present in one of the predicted genomic island regions of the large chromosome of V. cholerae O395 showing a strong homology with a conserved phage encoded protein. In-silico physicochemical analysis revealed that the hypothetical protein was a periplasmic protein. Homology modeling study indicated that the hypothetical protein was an unconventional and atypical serine protease belonging to HtrA protein family. The predicted 3D-model of the hypothetical protein revealed a catalytic centre serine utilizing a single catalytic residue for proteolysis. The predicted catalytic triad may
help to deduce the active site for the recruitment of the substrate for proteolysis. The active site arrangements of this predicted serine protease homologue with atypical catalytic triad is expected to allow these proteases to work in different environments of the host.
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| Date |
2013
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/1938/1/PLOS_ONE___8_(2_)____Article_Number_e56725;2013[73].pdf
Dutta, Avirup and Katarkar, Atul and Chaudhuri, Keya (2013) In-Silico Structural and Functional Characterization of a V. cholerae O395 Hypothetical Protein Containing a PDZ1 and an Uncommon Protease Domain. PLOS ONE, 8 (2). e56725. |
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| Relation |
http://dx.doi.org/10.1371/journal.pone.0056725
http://www.eprints.iicb.res.in/1938/ |
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