کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8384144 1543463 2008 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure
چکیده انگلیسی
Helicobacter pylori produces a heat shock protein A (HspA) that is unique to this bacteria. While the first 91 residues (domain A) of the protein are similar to GroES, the last 26 (domain B) are unique to HspA. Domain B contains eight histidines and four cysteines and was suggested to bind nickel. We have produced HspA and two mutants: Cys94Ala and Cys94Ala/Cys111Ala and identified the disulfide bridge pattern of the protein. We found that the cysteines are engaged in three disulfide bonds: Cys51/Cys53, Cys94/Cys111 and Cys95/Cys112 that result in a unique closed loop structure for the domain B.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 582, Issues 23–24, 15 October 2008, Pages 3537-3541
نویسندگان
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