About: Monomeric Camelus dromedarius GSTM1 at low pH is structurally more thermostable than its native dimeric form

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About: Monomeric Camelus dromedarius GSTM1 at low pH is structurally more thermostable than its native dimeric form Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Monomeric Camelus dromedarius GSTM1 at low pH is structurally more thermostable than its native dimeric form
Creator	Fouad, Dalia Malik, Ajamaluddin Abdelkader, Mohamed Alamery, Salman Ataya, Farid Daoud, Mohamed Khan, Javed Labrouid, Nikolaos
Source	PMC
abstract	Glutathione S‒transferases (GSTs) are multifunctional enzymes that play an important role in detoxification, cellular signalling, and the stress response. Camelus dromedarius is well-adapted to survive in extreme desert climate and it has GSTs, for which limited information is available. This study investigated the structure-function and thermodynamic properties of a mu-class camel GST (CdGSTM1) at different pH. Recombinant CdGSTM1 (25.7 kDa) was expressed in E. coli and purified to homogeneity. Dimeric CdGSTM1 dissociated into stable but inactive monomeric subunits at low pH. Conformational and thermodynamic changes during the thermal unfolding pathway of dimeric and monomeric CdGSTM1 were characterised via a thermal shift assay and dynamic multimode spectroscopy (DMS). The thermal shift assay based on intrinsic tryptophan fluorescence revealed that CdGSTM1 underwent a two-state unfolding pathway at pH 1.0–10.0. Its Tm value varied with varying pH. Another orthogonal technique based on far-UV CD also exhibited two-state unfolding in the dimeric and monomeric states. Generally, proteins tend to lose structural integrity and stability at low pH; however, monomeric CdGSTM1 at pH 2.0 was thermally more stable and unfolded with lower van't Hoff enthalpy. The present findings provide essential information regarding the structural, functional, and thermodynamic properties of CdGSTM1 at pH 1.0–10.0.
has issue date	2018-10-10(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0205274
bibo:pmid	30303997
has license	cc-by
sha1sum (hex)	bc01fae970a5c27f2213ac75db374170444545f6
schema:url	https://doi.org/10.1371/journal.pone.0205274
resource representing a document's title	Monomeric Camelus dromedarius GSTM1 at low pH is structurally more thermostable than its native dimeric form
has PubMed Central identifier	PMC6179282
has PubMed identifier	30303997
schema:publication	PLoS One
resource representing a document's body	covid:bc01fae970a5c27f2213ac75db374170444545f6#body_text
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