Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus

Biochimie
Danila LimauroSimonetta Bartolucci

Abstract

The detoxification from peroxides in Sulfolobus solfataricus is performed by the Bacterioferritin comigratory proteins (Bcps), Bcp1 (Sso2071), Bcp2 (Sso2121), Bcp3 (Sso2255) and Bcp4 (Sso2613), antioxidant enzymes belonging to one of the subfamilies of the Peroxiredoxins. In this paper we report on the functional, structural and docking analyses of Bcp4, characterized by the CXXXXC motif in the active site. Bcp4 represents the first dimeric Bcp so far investigated. Biochemical studies showed that the protein has a non-covalent dimeric structure and adopts an atypical 2-Cys catalytic mechanism. The X-ray structure of the double mutant C45S/C50S, representative of the fully reduced enzyme state, described the protein dimeric arrangement. Finally, concurrent availability of the crystallographic structure of the monomeric Bcp1 allowed comparative analysis of the interaction with Protein Disulfide Oxidoreductase SsPDO (Sso0192), involved in the reduction of both Bcp1 and Bcp4, through a protein-protein docking approach.

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Citations

Aug 30, 2012·Biochemistry·Arden PerkinsP Andrew Karplus
Dec 7, 2013·Extremophiles : Life Under Extreme Conditions·Danila LimauroEmilia Pedone
Mar 3, 2017·Extremophiles : Life Under Extreme Conditions·Jae Kyu LimHyun Sook Lee
Apr 11, 2018·Antioxidants & Redox Signaling·David YoungJoris Messens
Jun 18, 2019·Acta Crystallographica. Section F, Structural Biology Communications·Sander StroobantsEveline Peeters
May 10, 2020·Antioxidants·Mamta Rawat, Julie A Maupin-Furlow
Nov 28, 2017·Extremophiles : Life Under Extreme Conditions·Francesca Anna FuscoDanila Limauro
Aug 7, 2020·Antioxidants·Emilia PedoneDanila Limauro
Mar 9, 2018·International Journal of Biological Macromolecules·Francesca Anna FuscoDanila Limauro
Jul 1, 2018·New Biotechnology·Mariamichela LanzilliRachele Isticato

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