Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus

Abstract Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the polar residues. The primary role of these residues...

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Autores principales:	Sahini Banerjee, Parth Sarthi Sen Gupta, Rifat Nawaz Ul Islam, Amal Kumar Bandyopadhyay
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eb709fb6a7a34864b0ace9527010abca
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spelling	oai:doaj.org-article:eb709fb6a7a34864b0ace9527010abca2021-12-02T17:51:13ZIntrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus10.1038/s41598-021-90723-42045-2322https://doaj.org/article/eb709fb6a7a34864b0ace9527010abca2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90723-4https://doaj.org/toc/2045-2322Abstract Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the polar residues. The primary role of these residues is to enhance the salt-bridges and their ME. Unlike HuP, PfP has made many changes in its intrinsic property to strengthen the salt-bridge. First, the desolvation energy is reduced by directing the salt-bridge towards the surface. Second, it has made bridge-energy more favorable by recruiting energetically advantageous partners with high helix-propensity among the six possible salt-bridge pairs. Third, ME-residues that perform intricate interactions have increased their energy contribution by making major changes in their binary properties. The use of salt-bridge partners as ME-residues, and ME-residues' overlapping usage, predominant in helices, and energetically favorable substitution are some of the favorable features of PfP compared to HuP. These changes in PfP reduce the unfavorable, increase the favorable ME-energy. Thus, the per salt-bridge stability of PfP is greater than that of HuP. Further, unfavorable target ME-residues can be identified whose mutation can increase the stability of salt-bridge. The study applies to other similar systems.Sahini BanerjeeParth Sarthi Sen GuptaRifat Nawaz Ul IslamAmal Kumar BandyopadhyayNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sahini Banerjee Parth Sarthi Sen Gupta Rifat Nawaz Ul Islam Amal Kumar Bandyopadhyay Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
description	Abstract Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the polar residues. The primary role of these residues is to enhance the salt-bridges and their ME. Unlike HuP, PfP has made many changes in its intrinsic property to strengthen the salt-bridge. First, the desolvation energy is reduced by directing the salt-bridge towards the surface. Second, it has made bridge-energy more favorable by recruiting energetically advantageous partners with high helix-propensity among the six possible salt-bridge pairs. Third, ME-residues that perform intricate interactions have increased their energy contribution by making major changes in their binary properties. The use of salt-bridge partners as ME-residues, and ME-residues' overlapping usage, predominant in helices, and energetically favorable substitution are some of the favorable features of PfP compared to HuP. These changes in PfP reduce the unfavorable, increase the favorable ME-energy. Thus, the per salt-bridge stability of PfP is greater than that of HuP. Further, unfavorable target ME-residues can be identified whose mutation can increase the stability of salt-bridge. The study applies to other similar systems.
format	article
author	Sahini Banerjee Parth Sarthi Sen Gupta Rifat Nawaz Ul Islam Amal Kumar Bandyopadhyay
author_facet	Sahini Banerjee Parth Sarthi Sen Gupta Rifat Nawaz Ul Islam Amal Kumar Bandyopadhyay
author_sort	Sahini Banerjee
title	Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
title_short	Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
title_full	Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
title_fullStr	Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
title_full_unstemmed	Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus
title_sort	intrinsic basis of thermostability of prolyl oligopeptidase from pyrococcus furiosus
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/eb709fb6a7a34864b0ace9527010abca
work_keys_str_mv	AT sahinibanerjee intrinsicbasisofthermostabilityofprolyloligopeptidasefrompyrococcusfuriosus AT parthsarthisengupta intrinsicbasisofthermostabilityofprolyloligopeptidasefrompyrococcusfuriosus AT rifatnawazulislam intrinsicbasisofthermostabilityofprolyloligopeptidasefrompyrococcusfuriosus AT amalkumarbandyopadhyay intrinsicbasisofthermostabilityofprolyloligopeptidasefrompyrococcusfuriosus
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Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus

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