کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2828655 1162745 2012 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) from bovine muscle
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) from bovine muscle
چکیده انگلیسی

The SERCA pump, a membrane protein of about 110 kDa, transports two Ca2+ ions per ATP hydrolyzed from the cytoplasm to the lumen of the sarcoplasmic reticulum. In muscle cells, its ability to remove Ca2+ from the cytosol induces relaxation. The transport mechanism employed by the enzyme from rabbit muscle has been extensively studied, and several crystal structures representing different conformational states are available. However, no structure of the pump from other sources is known. In this paper we describe the crystal structure of the bovine enzyme, crystallized in the E1 conformation and determined at 2.9 Å resolution. The overall molecular model is very similar to that of the rabbit enzyme, as expected by the high amino acid sequence identity. Nevertheless, the bovine enzyme has reduced catalytic activity with respect to the rabbit enzyme. Subtle structural modifications, in particular in the region of the long loop that protrudes into the SR lumen connecting transmembrane α-helices M7 and M8, may explain the difference.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 178, Issue 1, April 2012, Pages 38–44
نویسندگان
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