کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298526 | 1537030 | 2018 | 26 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain
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کلمات کلیدی
Decyl maltosidek-PathDOCDDMPDBFCCPCCOSteroids - استروئیدdocosahexaenoic acid - اسید داکوزاگزوائونیکDHA - دوکوساهگزائنوئیک اسیدdeoxycholate - دگزیکسولاتRetinoic acid - رتینوئیک اسیدcytochrome c oxidase - سیتوکروم سی اکسیدازwild type - نوع وحشیDetergents - پاک کننده هاProtein Data Bank - پروتئین بانک اطلاعاتیLipids - چربیهاCarbonyl cyanide-4-(trifluoromethoxy)phenylhydrazone - کربونیل سیانید 4- (trifluoromethoxy) phenylhydrazone
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain](/preview/png/8298526.png)
چکیده انگلیسی
Three mutant forms of Rhodobacter sphaeroides cytochrome c oxidase (RsCcO) were created to test for multiple K-path entry sites (E101W), the existence of an “upper ligand site” (M350â¯W), and the nature and binding specificity of the “lower ligand site” (P315W/E101A) in the region of a crystallographically-defined deoxycholate at the K-path entrance. The effects of inhibitory and stimulatory detergents (dodecyl maltoside and Tween20) on these mutants are presented, as well as competition with other ligands, including the potentially physiologically relevant ligands cholesterol and retinoic acid. Ligands are shown to be able to compete with natural lipids to affect the activity of membrane-bound RsCcO. Results point to a single K-path entrance site at E101, with a single ligand binding pocket proximal to the entrance. The affinity of this pocket for amphipathic ligands is enhanced by removal of the E101 carboxyl and blocked by substituting a tryptophan in this area. A new crystal structure of the E101A mutant of RsCcO is presented that illustrates the structural basis of these results, showing that the loss of the E101 carboxyl creates a more hydrophobic groove consistent with altered ligand affinities.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1859, Issue 9, September 2018, Pages 725-733
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1859, Issue 9, September 2018, Pages 725-733
نویسندگان
Carrie Hiser, Jian Liu, Shelagh Ferguson-Miller,