کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914520 | 1162741 | 2012 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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چکیده انگلیسی
The F1FO-ATP synthase is a rotary molecular nanomotor. F1 is a chemical motor driven by ATP hydrolysis while FO is an electrical motor driven by the proton flow. The two stepping motors are mechanically coupled through a common rotary shaft. Up to now, the three available crystal structures of the F1c10 sub-complex of the yeast F1FO-ATP synthase were isomorphous and then named yF1c10(I). In this crystal form, significant interactions of the c10-ring with the F1-head of neighboring molecules affected the overall conformation of the F1-c-ring complex. The symmetry axis of the F1-head and the inertia axis of the c-ring were tilted near the interface between the F1-central stalk and the c-ring rotor, resulting in an unbalanced machine. We have solved a new crystal form of the F1c10 complex, named yF1c10(II), inhibited by adenylyl-imidodiphosphate (AMP-PNP) and dicyclohexylcarbodiimide (DCCD), at 6.5Â Ã
resolution in which the crystal packing has a weaker influence over the conformation of the F1-c-ring complex. yF1c10(II) provides a model of a more efficient generator. yF1c10(II) and bovine bF1c8 structures share a common rotor architecture with the inertia center of the F1-stator close to the rotor axis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 177, Issue 2, February 2012, Pages 490-497
Journal: Journal of Structural Biology - Volume 177, Issue 2, February 2012, Pages 490-497
نویسندگان
Marie-France Giraud, Patrick Paumard, Corinne Sanchez, Daniel Brèthes, Jean Velours, Alain Dautant,