کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8295240 1536758 2018 25 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Solution structure analysis of the periplasmic region of bacterial flagellar motor stators by small angle X-ray scattering
ترجمه فارسی عنوان
تجزیه و تحلیل ساختار راه حل ناحیه پری پلاسمی استاکر موتورهای باکتریایی با پراکندگی اشعه ایکس زاویه کوچک
کلمات کلیدی
موتور ضایعه باکتریایی، پراکندگی اشعه ایکس زاویه کوچک، زیست شناسی ساختاری، مجامع مغناطیسی، کمبود اکسیژن باکتریایی پروتئین اتصال پپتیدوگلیکان،
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
The bacterial flagellar motor drives the rotation of helical flagellar filaments to propel bacteria through viscous media. It consists of a dynamic population of mechanosensitive stators that are embedded in the inner membrane and activate in response to external load. This entails assembly around the rotor, anchoring to the peptidoglycan layer to counteract torque from the rotor and opening of a cation channel to facilitate an influx of cations, which is converted into mechanical rotation. Stator complexes are comprised of four copies of an integral membrane A subunit and two copies of a B subunit. Each B subunit includes a C-terminal OmpA-like peptidoglycan-binding (PGB) domain. This is thought to be linked to a single N-terminal transmembrane helix by a long unstructured peptide, which allows the PGB domain to bind to the peptidoglycan layer during stator anchoring. The high-resolution crystal structures of flagellar motor PGB domains from Salmonella enterica (MotBC2) and Vibrio alginolyticus (PomBC5) have previously been elucidated. Here, we use small-angle X-ray scattering (SAXS). We show that unlike MotBC2, the dimeric conformation of the PomBC5 in solution differs to its crystal structure, and explore the functional relevance by characterising gain-of-function mutants as well as wild-type constructs of various lengths. These provide new insight into the conformational diversity of flagellar motor PGB domains and experimental verification of their overall topology.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 495, Issue 2, 8 January 2018, Pages 1614-1619
نویسندگان
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