Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions (840 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2009 Mar; 1794(3): 554-562.
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Paper type: Journal Article,
Impact factor: 2.48, 5-year impact factor: 2.993
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-59349103950&partnerID=40&md5=ca16aa7d74ce0720028e8d04c27ae01c
Keywords: Archaea, Cofactor Binding, Nadh Oxidase, Oxidoreductase, Protein Function And Stability, Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase, Thioredoxin Reductase, Article, Circular Dichroism, Crystal Structure, Denaturation, Enzyme Isolation, Enzyme Structure, Priority Journal, Protein Analysis, Protein Stability, Protein Structure, Sulfolobus Solfataricus, Thermostability, Wild Type, Amino Acid Sequence, Binding Sites, Disulfides, Enzyme Stability, Flavin-Adenine Dinucleotide, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Thioredoxin-Disulfide Reductase,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy
Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Roccelletta di Borgia, I-88021 Catanzaro, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Via S. Pansini 5, I-80131 Napoli, Italy
Dipartimento delle Scienze Biologiche, Sezione di Biostrutture, Università degli Studi di Napoli Federico II, Via Mezzocannone 16, I-80134 Napoli, Italy
CEINGE Biotecnologie Avanzate s.c.a r.l., Via Comunale Margherita 482, I-80145 Napoli, Italy
References:
Not available.
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2009 Mar; 1794(3): 554-562.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.48, 5-year impact factor: 2.993
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-59349103950&partnerID=40&md5=ca16aa7d74ce0720028e8d04c27ae01c
Keywords: Archaea, Cofactor Binding, Nadh Oxidase, Oxidoreductase, Protein Function And Stability, Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase, Thioredoxin Reductase, Article, Circular Dichroism, Crystal Structure, Denaturation, Enzyme Isolation, Enzyme Structure, Priority Journal, Protein Analysis, Protein Stability, Protein Structure, Sulfolobus Solfataricus, Thermostability, Wild Type, Amino Acid Sequence, Binding Sites, Disulfides, Enzyme Stability, Flavin-Adenine Dinucleotide, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Thioredoxin-Disulfide Reductase,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy
Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Roccelletta di Borgia, I-88021 Catanzaro, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Via S. Pansini 5, I-80131 Napoli, Italy
Dipartimento delle Scienze Biologiche, Sezione di Biostrutture, Università degli Studi di Napoli Federico II, Via Mezzocannone 16, I-80134 Napoli, Italy
CEINGE Biotecnologie Avanzate s.c.a r.l., Via Comunale Margherita 482, I-80145 Napoli, Italy
References:
Not available.
Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions
Recent investigations have demonstrated that disulfide bridges may play a crucial role in the stabilization of proteins in hyperthermophilic organisms. A major role in the process of disulfide formation is played by ubiquitous proteins belonging to the thioredoxin superfamily, which includes thioredoxins (Trx), thioredoxin reductases (TrxR), and disulfide oxidases/isomerases (PDO/PDI). Here we report a characterization of the structure and stability of the TrxR (SsTrxRB3) isolated from the archaeon Sulfolobus solfataricus. This protein is particularly interesting since it is able to process different substrates (Trxs and PDO) and it is endowed with an additional NADH oxidase activity. The crystal structure of the wild-type enzyme, of its complex with NADP and of the C147A mutant provides interesting clues on the enzyme function. In contrast to what is observed for class II TrxRs, in the structure of the oxidized enzyme, the FAD binding site is occupied by a partially disordered NAD molecule. In the active site of the C147A mutant, which exhibits a marginal NADH oxidase activity, the FAD is canonically bound to the enzyme. Molecular modeling indicates that a FAD molecule can be accommodated in the site of the reduced SsTrxRB3. Depending on the oxidation state, SsTrxRB3 can bind a different cofactor in its active site. This peculiar feature has been related to its dual activity. Denaturation experiments followed by circular dichroism indicate that electrostatic interactions play an important role in the stabilization of this thermostable protein. The analysis of the enzyme 3D-structure has also provided insights into the bases of SsTrxRB3 stability. (C) 2008 Elsevier B.V. All rights reserved.
Recent investigations have demonstrated that disulfide bridges may play a crucial role in the stabilization of proteins in hyperthermophilic organisms. A major role in the process of disulfide formation is played by ubiquitous proteins belonging to the thioredoxin superfamily, which includes thioredoxins (Trx), thioredoxin reductases (TrxR), and disulfide oxidases/isomerases (PDO/PDI). Here we report a characterization of the structure and stability of the TrxR (SsTrxRB3) isolated from the archaeon Sulfolobus solfataricus. This protein is particularly interesting since it is able to process different substrates (Trxs and PDO) and it is endowed with an additional NADH oxidase activity. The crystal structure of the wild-type enzyme, of its complex with NADP and of the C147A mutant provides interesting clues on the enzyme function. In contrast to what is observed for class II TrxRs, in the structure of the oxidized enzyme, the FAD binding site is occupied by a partially disordered NAD molecule. In the active site of the C147A mutant, which exhibits a marginal NADH oxidase activity, the FAD is canonically bound to the enzyme. Molecular modeling indicates that a FAD molecule can be accommodated in the site of the reduced SsTrxRB3. Depending on the oxidation state, SsTrxRB3 can bind a different cofactor in its active site. This peculiar feature has been related to its dual activity. Denaturation experiments followed by circular dichroism indicate that electrostatic interactions play an important role in the stabilization of this thermostable protein. The analysis of the enzyme 3D-structure has also provided insights into the bases of SsTrxRB3 stability. (C) 2008 Elsevier B.V. All rights reserved.
Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions
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Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
View Export to BibTeX Export to EndNote
D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
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Impact Factor: 4.89
View Export to BibTeX Export to EndNote
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Impact Factor: 4.89
View Export to BibTeX Export to EndNote
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Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2004 Nov; 60(11): 2076-2077.
Impact Factor: 1.693
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Pedone E, Bartolucci S, Fiorentino G
* Sensing and adapting to environmental stress: The Archaeal tactic (592 views)
Frontiers In Bioscience (ISSN: 1093-9946, 1093-4715), 2004 Sep 1; 9: 2909-2926.
Impact Factor: 3.226
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Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (716 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
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D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
* Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione (1343 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003 Jun; 59: 1043-1045.
Impact Factor: 2.208
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Garzillo AM, Colao MC, Buonocore V, Oliva R, Falcigno L, Saviano M, Santoro AM, Zappala R, Bonomo RP, Bianco C, Giardina P, Palmieri G, Sannia G
* Structural and kinetic characterization of native laccases from Pleurotas ostreatus, Rigidoporus lignosus, and Trametes trogii (983 views)
Journal Of Protein Chemistry (ISSN: 0277-8033), 2001 Apr; 20(3): 191-201.
Impact Factor: 1.021
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Bonomo RP, Cennamo G, Purrello R, Santoro AM, Zappala R
* Comparison Of Three Fungal Laccases From Rigidoporus Lignosus And Pleurotus Ostreatus: Correlation Between Conformation Changes And Catalytic Activity (593 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2001 Jan 1; 83(1): 67-75.
Impact Factor: 1.729
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Cambria M, Cambria A, Ragusa S, Rizzarelli E
Production, purification, and properties of an extracellular laccase from Rigidoporus lignosus (621 views)
Protein Expr Purif (ISSN: 1046-5928), 2000 Mar; 18(2): 141-147.
Impact Factor: 1.569
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Bonomo RP, Boudet AM, Cozzolino R, Rizzarelli E, Santoro AM, Sterjiades R, Zappalà R
A comparative study of two isoforms of laccase secreted by the 'white- rot' fungus Rigidoporus lignosus, exhibiting significant structural and functional differences (709 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1998 Sep; 71(3-4): 205-211.
Impact Factor: 1.162
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28 Records (27 excluding Abstracts).
Total impact factor: 97.365 (94.483 excluding Abstracts).
Total 5 year impact factor: 117.301 (114.419 excluding Abstracts).
Total impact factor: 97.365 (94.483 excluding Abstracts).
Total 5 year impact factor: 117.301 (114.419 excluding Abstracts).
840 views. Last view on Wednesday 16 April 2025, 19:40:23
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