کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914525 | 1162741 | 2012 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability
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کلمات کلیدی
RMSDPDBTrxTrxRGuHClX-ray crystallography - بلورنگاری پرتو-ایکسthioredoxin reductase - تریودوکسین ردوکتازthioredoxin - تیرودوکسینChemical denaturation - دینامیک شیمیاییcircular dichroism - رنگ تابی دورانیProtein structure-function - ساختار تابع پروتئینroot mean square deviation - میانگین انحراف مربع ریشهProtein Data Bank - پروتئین بانک اطلاعاتیDisulfide bonds - پیوند های دی سولفیدGuanidine hydrochloride - گوانیدین هیدروکلراید
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability](/preview/png/5914525.png)
چکیده انگلیسی
Structural characterizations of thioredoxins (Trxs) are important for their involvement in severe pathologies and for their stable scaffold. Here we report a combined structural and spectroscopic characterization of a Trx isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (SsTrxA1). Thermal denaturation unveils that SsTrxA1 is endowed with a remarkable stability in the explored temperature range 50-105 °C. The structure of the oxidized form of SsTrxA1 determined at 1.9 Ã
resolution presents a number of peculiar features. Although the protein was crystallized in a slightly acid medium (pH 6.5) as many as ten intramolecular/intermolecular carboxyl-carboxylate interactions involving glutamic and aspartic acid side chains are found in three independent SsTrxA1 molecules present in the asymmetric unit. Surprisingly for a hyperthermostable protein, the structure of SsTrxA1 is characterized by the presence (a) of a very limited number of intramolecular salt bridges and (b) of a cavity nearby Cys52, a residue that is frequently a phenylananine in other members of the family. Chemical denaturation investigations carried out on SsTrxA1 and SsTrxA2 show that both proteins present a significant stability against guanidine hydrochloride, thus indicating that ionic interactions play a minor role in their stabilization. Compared to Trxs from mesophilic sources, SsTrxA1 displays a longer α-helix 1 and a shorter loop connecting this α-helix with β-strand 2. As these features are shared with Trxs isolated from thermophilic sources, the shortening of this loop may be a general strategy adopted to stabilize this fold. This feature may be exploited for the design of hyperthermostable Trx scaffolds.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 177, Issue 2, February 2012, Pages 506-512
Journal: Journal of Structural Biology - Volume 177, Issue 2, February 2012, Pages 506-512
نویسندگان
Luciana Esposito, Alessia Ruggiero, Mariorosario Masullo, Maria Rosaria Ruocco, Anna Lamberti, Paolo Arcari, Adriana Zagari, Luigi Vitagliano,