Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8
It is hypothesized that the Ca2+ ions were involved in the activity, folding and stabilization of many protein structures. Many of these proteins contain repeat in toxin (RTX) motifs. AMS8 lipase from Antarctic Pseudomonas fluorescens strain AMS8 was found to have three RTX motifs. So, this research...
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ftmdpi:oai:mdpi.com:/2072-6651/12/1/27/ 2023-08-20T04:02:00+02:00 Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 Nur Shidaa Mohd Ali Abu Bakar Salleh Raja Noor Zaliha Raja Abd Rahman Thean Chor Leow Mohd Shukuri Mohamad Ali agris 2020-01-01 application/pdf https://doi.org/10.3390/toxins12010027 EN eng Multidisciplinary Digital Publishing Institute Bacterial Toxins https://dx.doi.org/10.3390/toxins12010027 https://creativecommons.org/licenses/by/4.0/ Toxins; Volume 12; Issue 1; Pages: 27 RTX lipase AMS8 lipase family I.3 RTX parallel β -roll motif repeat Ca 2+ ion calcium binding folding activity Text 2020 ftmdpi https://doi.org/10.3390/toxins12010027 2023-07-31T22:57:29Z It is hypothesized that the Ca2+ ions were involved in the activity, folding and stabilization of many protein structures. Many of these proteins contain repeat in toxin (RTX) motifs. AMS8 lipase from Antarctic Pseudomonas fluorescens strain AMS8 was found to have three RTX motifs. So, this research aimed to examine the influence of Ca2+ ion towards the activity and folding of AMS8 lipase through various biophysical characterizations. The results showed that CaCl2 increased lipase activity. The far-UV circular dichroism (CD) and Fourier-transform infrared (FTIR) analysis suggested that the secondary structure content was improved with the addition of CaCl2. Fluorescence spectroscopy analysis showed that the presence of CaCl2 increased protein folding and compactness. Dynamic light scattering (DLS) analysis suggested that AMS8 lipase became aggregated at a high concentration of CaCl2.The binding constant (Kd) value from the isothermal titration calorimetry (ITC) analysis proved that the Ca2+ ion was tightly bound to the AMS8 lipase. In conclusion, Ca2+ ions play crucial roles in the activity and folding of the AMS8 lipase. Calcium binding to RTX nonapeptide repeats sequences will induced the formation and folding of the RTX parallel β-roll motif repeat structure. Text Antarc* Antarctic MDPI Open Access Publishing Antarctic Toxins 12 1 27 |
institution |
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MDPI Open Access Publishing |
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ftmdpi |
language |
English |
topic |
RTX lipase AMS8 lipase family I.3 RTX parallel β -roll motif repeat Ca 2+ ion calcium binding folding activity |
spellingShingle |
RTX lipase AMS8 lipase family I.3 RTX parallel β -roll motif repeat Ca 2+ ion calcium binding folding activity Nur Shidaa Mohd Ali Abu Bakar Salleh Raja Noor Zaliha Raja Abd Rahman Thean Chor Leow Mohd Shukuri Mohamad Ali Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
topic_facet |
RTX lipase AMS8 lipase family I.3 RTX parallel β -roll motif repeat Ca 2+ ion calcium binding folding activity |
description |
It is hypothesized that the Ca2+ ions were involved in the activity, folding and stabilization of many protein structures. Many of these proteins contain repeat in toxin (RTX) motifs. AMS8 lipase from Antarctic Pseudomonas fluorescens strain AMS8 was found to have three RTX motifs. So, this research aimed to examine the influence of Ca2+ ion towards the activity and folding of AMS8 lipase through various biophysical characterizations. The results showed that CaCl2 increased lipase activity. The far-UV circular dichroism (CD) and Fourier-transform infrared (FTIR) analysis suggested that the secondary structure content was improved with the addition of CaCl2. Fluorescence spectroscopy analysis showed that the presence of CaCl2 increased protein folding and compactness. Dynamic light scattering (DLS) analysis suggested that AMS8 lipase became aggregated at a high concentration of CaCl2.The binding constant (Kd) value from the isothermal titration calorimetry (ITC) analysis proved that the Ca2+ ion was tightly bound to the AMS8 lipase. In conclusion, Ca2+ ions play crucial roles in the activity and folding of the AMS8 lipase. Calcium binding to RTX nonapeptide repeats sequences will induced the formation and folding of the RTX parallel β-roll motif repeat structure. |
format |
Text |
author |
Nur Shidaa Mohd Ali Abu Bakar Salleh Raja Noor Zaliha Raja Abd Rahman Thean Chor Leow Mohd Shukuri Mohamad Ali |
author_facet |
Nur Shidaa Mohd Ali Abu Bakar Salleh Raja Noor Zaliha Raja Abd Rahman Thean Chor Leow Mohd Shukuri Mohamad Ali |
author_sort |
Nur Shidaa Mohd Ali |
title |
Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
title_short |
Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
title_full |
Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
title_fullStr |
Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
title_full_unstemmed |
Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
title_sort |
calcium-induced activity and folding of a repeat in toxin lipase from antarctic pseudomonas fluorescens strain ams8 |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2020 |
url |
https://doi.org/10.3390/toxins12010027 |
op_coverage |
agris |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Toxins; Volume 12; Issue 1; Pages: 27 |
op_relation |
Bacterial Toxins https://dx.doi.org/10.3390/toxins12010027 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/toxins12010027 |
container_title |
Toxins |
container_volume |
12 |
container_issue |
1 |
container_start_page |
27 |
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1774712383699156992 |