Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8
It is hypothesized that the Ca(2+) 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 resear...
Published in: | Toxins |
---|---|
Main Authors: | , , , , |
Format: | Text |
Language: | English |
Published: |
MDPI
2020
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020413/ http://www.ncbi.nlm.nih.gov/pubmed/31906409 https://doi.org/10.3390/toxins12010027 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:7020413 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:7020413 2023-05-15T13:49:15+02:00 Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 Ali, Nur Shidaa Mohd Salleh, Abu Bakar Rahman, Raja Noor Zaliha Raja Abd Leow, Thean Chor Ali, Mohd Shukuri Mohamad 2020-01-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020413/ http://www.ncbi.nlm.nih.gov/pubmed/31906409 https://doi.org/10.3390/toxins12010027 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020413/ http://www.ncbi.nlm.nih.gov/pubmed/31906409 http://dx.doi.org/10.3390/toxins12010027 © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2020 ftpubmed https://doi.org/10.3390/toxins12010027 2020-03-15T01:22:45Z It is hypothesized that the Ca(2+) 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 Ca(2+) ion towards the activity and folding of AMS8 lipase through various biophysical characterizations. The results showed that CaCl(2) 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 CaCl(2). Fluorescence spectroscopy analysis showed that the presence of CaCl(2) increased protein folding and compactness. Dynamic light scattering (DLS) analysis suggested that AMS8 lipase became aggregated at a high concentration of CaCl(2).The binding constant (K(d)) value from the isothermal titration calorimetry (ITC) analysis proved that the Ca(2+) ion was tightly bound to the AMS8 lipase. In conclusion, Ca(2+) 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 PubMed Central (PMC) Antarctic Toxins 12 1 27 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Article |
spellingShingle |
Article Ali, Nur Shidaa Mohd Salleh, Abu Bakar Rahman, Raja Noor Zaliha Raja Abd Leow, Thean Chor Ali, Mohd Shukuri Mohamad Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 |
topic_facet |
Article |
description |
It is hypothesized that the Ca(2+) 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 Ca(2+) ion towards the activity and folding of AMS8 lipase through various biophysical characterizations. The results showed that CaCl(2) 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 CaCl(2). Fluorescence spectroscopy analysis showed that the presence of CaCl(2) increased protein folding and compactness. Dynamic light scattering (DLS) analysis suggested that AMS8 lipase became aggregated at a high concentration of CaCl(2).The binding constant (K(d)) value from the isothermal titration calorimetry (ITC) analysis proved that the Ca(2+) ion was tightly bound to the AMS8 lipase. In conclusion, Ca(2+) 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 |
Ali, Nur Shidaa Mohd Salleh, Abu Bakar Rahman, Raja Noor Zaliha Raja Abd Leow, Thean Chor Ali, Mohd Shukuri Mohamad |
author_facet |
Ali, Nur Shidaa Mohd Salleh, Abu Bakar Rahman, Raja Noor Zaliha Raja Abd Leow, Thean Chor Ali, Mohd Shukuri Mohamad |
author_sort |
Ali, Nur Shidaa Mohd |
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 |
MDPI |
publishDate |
2020 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020413/ http://www.ncbi.nlm.nih.gov/pubmed/31906409 https://doi.org/10.3390/toxins12010027 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020413/ http://www.ncbi.nlm.nih.gov/pubmed/31906409 http://dx.doi.org/10.3390/toxins12010027 |
op_rights |
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.3390/toxins12010027 |
container_title |
Toxins |
container_volume |
12 |
container_issue |
1 |
container_start_page |
27 |
_version_ |
1766251046619840512 |