Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism

Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entrop...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Nehad Noby, Husam Sabah Auhim, Samuel Winter, Harley L. Worthy, Amira M. Embaby, Hesham Saeed, Ahmed Hussein, Christopher R. Pudney, Pierre J. Rizkallah, Stephen A. Wells, D. Dafydd Jones
Formato:	article
Lenguaje:	EN
Publicado:	The Royal Society 2021
Materias:	serine esterase molecular dynamics enzyme structure protein stability structure–function Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/742a9bfe43b248879d57a96a80adc331
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:742a9bfe43b248879d57a96a80adc331
record_format	dspace
spelling	oai:doaj.org-article:742a9bfe43b248879d57a96a80adc3312021-12-01T08:06:04ZStructure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism10.1098/rsob.2101822046-2441https://doaj.org/article/742a9bfe43b248879d57a96a80adc3312021-12-01T00:00:00Zhttps://royalsocietypublishing.org/doi/10.1098/rsob.210182https://doaj.org/toc/2046-2441Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical content providing greater access to the active site through more than one substrate access tunnel. However, dynamics do not appear to play a major role in cold adaption. Molecular dynamics at different temperatures, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are important for of EstN7's cold adaptation rather than changes in dynamics.Nehad NobyHusam Sabah AuhimSamuel WinterHarley L. WorthyAmira M. EmbabyHesham SaeedAhmed HusseinChristopher R. PudneyPierre J. RizkallahStephen A. WellsD. Dafydd JonesThe Royal Societyarticleserine esterasemolecular dynamicsenzyme structureprotein stabilitystructure–functionBiology (General)QH301-705.5ENOpen Biology, Vol 11, Iss 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	serine esterase molecular dynamics enzyme structure protein stability structure–function Biology (General) QH301-705.5
spellingShingle	serine esterase molecular dynamics enzyme structure protein stability structure–function Biology (General) QH301-705.5 Nehad Noby Husam Sabah Auhim Samuel Winter Harley L. Worthy Amira M. Embaby Hesham Saeed Ahmed Hussein Christopher R. Pudney Pierre J. Rizkallah Stephen A. Wells D. Dafydd Jones Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
description	Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical content providing greater access to the active site through more than one substrate access tunnel. However, dynamics do not appear to play a major role in cold adaption. Molecular dynamics at different temperatures, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are important for of EstN7's cold adaptation rather than changes in dynamics.
format	article
author	Nehad Noby Husam Sabah Auhim Samuel Winter Harley L. Worthy Amira M. Embaby Hesham Saeed Ahmed Hussein Christopher R. Pudney Pierre J. Rizkallah Stephen A. Wells D. Dafydd Jones
author_facet	Nehad Noby Husam Sabah Auhim Samuel Winter Harley L. Worthy Amira M. Embaby Hesham Saeed Ahmed Hussein Christopher R. Pudney Pierre J. Rizkallah Stephen A. Wells D. Dafydd Jones
author_sort	Nehad Noby
title	Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
title_short	Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
title_full	Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
title_fullStr	Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
title_full_unstemmed	Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
title_sort	structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
publisher	The Royal Society
publishDate	2021
url	https://doaj.org/article/742a9bfe43b248879d57a96a80adc331
work_keys_str_mv	AT nehadnoby structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT husamsabahauhim structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT samuelwinter structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT harleylworthy structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT amiramembaby structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT heshamsaeed structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT ahmedhussein structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT christopherrpudney structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT pierrejrizkallah structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT stephenawells structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism AT ddafyddjones structureandinsilicosimulationsofacoldactiveesteraserevealsitsprimecoldadaptationmechanism
_version_	1718405418983620608

Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism

Ejemplares similares