Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration
Abstract Glutaredoxin (GRXs) protein plays a vital role inside the cell, including redox control of transcription to the cell's antioxidant defense, apoptosis, and cellular differentiation regulation. In this study, we have investigated the energy landscape and characterized the pattern of loca...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Instituto Internacional de Ecologia
2023-09-01
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| Series: | Brazilian Journal of Biology |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842023000100850&lng=en&tlng=en |
| _version_ | 1797681721420808192 |
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| author | A. Patel K. Tiwari P. Asrani H. Alothaid A. F. A. Alahmari R. Mirdad M. R. Ajmal M. Tarique |
| author_facet | A. Patel K. Tiwari P. Asrani H. Alothaid A. F. A. Alahmari R. Mirdad M. R. Ajmal M. Tarique |
| author_sort | A. Patel |
| collection | DOAJ |
| description | Abstract Glutaredoxin (GRXs) protein plays a vital role inside the cell, including redox control of transcription to the cell's antioxidant defense, apoptosis, and cellular differentiation regulation. In this study, we have investigated the energy landscape and characterized the pattern of local frustration in different forms and states of the GRX protein ofE. coli.Analysis was done on the conformational alterations, significant changes in the frustration pattern, and different GRXs such as GRX-II, GRX-III, GRX-II-GSH, and GRX-III-GSH complex. We have found the practice of frustration, and structure was quite similar in the same isoform having different states of protein; however, a significant difference was observed between different isoforms. Moreover, oxidation of GRX-I introduced an extra α-helix increasing the destabilizing interactions within the protein. The study of frustrated contacts on oxidized and reduced GRX and with bound and unbound Glutathione indicates its potential application in activating and regulating the behavior of GRXs. |
| first_indexed | 2024-03-11T23:50:12Z |
| format | Article |
| id | doaj.art-69a96cfb6d234133ab25edd9ca6100bc |
| institution | Directory Open Access Journal |
| issn | 1678-4375 |
| language | English |
| last_indexed | 2024-03-11T23:50:12Z |
| publishDate | 2023-09-01 |
| publisher | Instituto Internacional de Ecologia |
| record_format | Article |
| series | Brazilian Journal of Biology |
| spelling | doaj.art-69a96cfb6d234133ab25edd9ca6100bc2023-09-19T07:44:35ZengInstituto Internacional de EcologiaBrazilian Journal of Biology1678-43752023-09-018310.1590/1519-6984.273091Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustrationA. Patelhttps://orcid.org/0000-0002-5320-3202K. Tiwarihttps://orcid.org/0000-0001-8630-4774P. Asranihttps://orcid.org/0000-0002-4747-4567H. Alothaidhttps://orcid.org/0000-0003-0132-558XA. F. A. Alahmarihttps://orcid.org/0009-0008-9250-9547R. Mirdadhttps://orcid.org/0009-0008-2388-2540M. R. Ajmalhttps://orcid.org/0000-0002-2480-9379M. Tariquehttps://orcid.org/0000-0002-0222-1339Abstract Glutaredoxin (GRXs) protein plays a vital role inside the cell, including redox control of transcription to the cell's antioxidant defense, apoptosis, and cellular differentiation regulation. In this study, we have investigated the energy landscape and characterized the pattern of local frustration in different forms and states of the GRX protein ofE. coli.Analysis was done on the conformational alterations, significant changes in the frustration pattern, and different GRXs such as GRX-II, GRX-III, GRX-II-GSH, and GRX-III-GSH complex. We have found the practice of frustration, and structure was quite similar in the same isoform having different states of protein; however, a significant difference was observed between different isoforms. Moreover, oxidation of GRX-I introduced an extra α-helix increasing the destabilizing interactions within the protein. The study of frustrated contacts on oxidized and reduced GRX and with bound and unbound Glutathione indicates its potential application in activating and regulating the behavior of GRXs.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842023000100850&lng=en&tlng=englutaredoxinsfrustration indexprotein stabilitystructure-function relationshipsbioinformaticsstructural biology |
| spellingShingle | A. Patel K. Tiwari P. Asrani H. Alothaid A. F. A. Alahmari R. Mirdad M. R. Ajmal M. Tarique Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration Brazilian Journal of Biology glutaredoxins frustration index protein stability structure-function relationships bioinformatics structural biology |
| title | Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration |
| title_full | Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration |
| title_fullStr | Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration |
| title_full_unstemmed | Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration |
| title_short | Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration |
| title_sort | glutaredoxin proteins from e coli isoforms were compared in terms of energy frustration |
| topic | glutaredoxins frustration index protein stability structure-function relationships bioinformatics structural biology |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842023000100850&lng=en&tlng=en |
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