http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14094
Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus (Articolo in rivista)
- Type
- Label
- Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/prot.22408 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- D'Ambrosio Katia; Limauro Danila; Pedone Emilia; Galdi Ilaria; Pedone Carlo; Bartolucci Simonetta; De Simone Giuseppina. (literal)
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- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Naples, Italy
Dipartimento di Biologia Strutturale e Funzionale, Universita` degli Studi di Napoli ''Federico II,'' Complesso Universitario Monte S. Angelo, Via Cinthia, 80126 Naples, Italy (literal)
- Titolo
- Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus (literal)
- Abstract
- Bcps constitute a group of antioxidant enzymes, belonging to the Prx family, that are widely distributed in bacteria, plants, and fungi. These proteins
can contain two conserved cysteines within the CXXXXC motif. Recent studies demonstrated that though the role of the first cysteine is well defined,
being the catalytic peroxidatic cysteine in all the members of this protein family, data on the function of the second cysteine are controversial and
require further investigation. In this article, we report on the functional and structural characterization of Bcp1, an archaeal Bcp isolated from
Sulfolobus solfataricus, which presents two conserved cysteine residues at positions 45 and 50. Functional studies revealed that this enzyme performs
the catalytic reaction using an atypical 2-Cys mechanism, where Cys45 is the peroxidatic and Cys50 is the resolving cysteine. The X-ray structure
of the double mutant C45S/C50S, representative of the fully reduced enzyme state, was determined at a resolution of 2.15 A ° , showing a Trx fold similar
to that of other Prxs. Superposition with a structural homologue in the oxidized state provided, for the first time, a detailed description of the structural
rearrangement necessary for a member of the Bcp family to perform the catalytic reaction. From this structural analysis, it emerges that a significant
conformational change from a fully folded, to a locally unfolded form is required to form the intramolecular disulfide bond upon oxidation, according
to the proposed reaction mechanism. Two residues, namely Arg53 and Asp54, which could play a role in this rearrangement, were also identified. (literal)
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