Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus(486 views) Ruggiero A, Lanzotti MA, Ruocco MR, Grimaldi P, Marasco D, Arcari P, Masullo M, Zagari A, Vitagliano L
Keywords: Hyperthermostability, Sulfolobus Solfataricus, Thioredoxins, Archaea, Archaeal Protein, Recombinant Protein, Amino Acid Sequence, Article, Chemistry, Crystallization, Dimerization, Genetics, Information Processing, Isolation And Purification, Molecular Genetics, Molecular Weight, Protein Stability, Protein Tertiary Structure, Sequence Homology, Statistics, Temperature, X Ray Crystallography, X Ray Diffraction, X-Ray, Data Collection, Molecular Sequence Data, Protein Structure, Statistics As Topic, X-Ray Diffraction,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy
Dipartimento Delle Scienze Biologiche, Sezione di Biostrutture, Universit Degli Studi di Napoli Federico II, Via Mezzocannone 16, I-80134 Napoli, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Universit Degli Studi di Napoli Federico II, Via S. Pansini 5, I-80131 Napoli, Italy
Dipartimento di Scienze Farmacobiologiche, Universit Degli Studi Magna Graecia di Catanzaro, Roccelletta di Borgia, I-88021 Catanzaro, Italy
CEINGE Biotecnologie Avanzate S.c.a.r.l., Via Comunale Margherita 482, I-80145 Napoli, Italy
CNISM Universit degli Studi di Napoli Federico II, Italy
References: Not available.
Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus
The thioredoxin system of the archaeon Sulfolobus solfataricus involves a number of different proteins: two thioredoxin reductases (SsTrxRB2 and SsTrxRB3), two distinct thioredoxins (SsTrxA1 and SsTrxA2) and a disulfide oxidoreductase (SsPDO). Here, the crystallization and preliminary crystallographic analyses of SsTrxA1 and SsTrxA2, two dimeric proteins endowed with extraordinary thermal stability, are reported. In addition to the functional thioredoxin domain, both SsTrxA1 and SsTrxA2 present an extra N-terminal fragment of approximately 30 residues. Although crystallization trials have been conducted on both forms of the proteins, crystals that were suitable for X-ray crystallographic analyses have only been obtained for their truncated variants. The crystals of SsTrxA2 belonged to space group P2, with unit-cell parameters a = 28.27, b = 27.88, c = 62.06 angstrom, beta = 92.34 degrees, and diffracted to 1.83 angstrom resolution, whereas the crystals of SsTrxA1 belonged to space group P2(1), with unit-cell parameters a = 51.76, b = 75.09, c = 55.35 angstrom, beta = 112.64 degrees, and diffracted to 1.90 angstrom resolution. The structures of the two proteins have been solved by molecular replacement.
Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus