کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5202495 | 1381901 | 2012 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76Â Ã
resolution
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
We determined the crystal structure of a cutinase from Thermobifida alba AHK119 (Est119) at a resolution of 1.76Â Ã
. The overall structure of Est119 displays a typical α/β-hydrolase fold consisting of a central twisted β-sheet of nine β-strands that are flanked by nine α-helices on both sides. The refined model contains two monomers in the asymmetric unit that form a dimer interface; a polyethylene glycol fragment is bound in the interface. Polyethylene glycol-binding site on the protein may suggest a glycol-binding site. A putative polymer-recognizing groove is observed to continue through the catalytic pocket. Water molecules are bound to hydrophilic amino acids along the groove, indicating the alternating pattern of polar and hydrophobic residues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Polymer Degradation and Stability - Volume 97, Issue 5, May 2012, Pages 771-775
Journal: Polymer Degradation and Stability - Volume 97, Issue 5, May 2012, Pages 771-775
نویسندگان
Kengo Kitadokoro, Uschara Thumarat, Ryota Nakamura, Kousuke Nishimura, Hajime Karatani, Hideyuki Suzuki, Fusako Kawai,