کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10795659 | 1052589 | 2014 | 16 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Functional and structural dynamics of NhaA, a prototype for Na+ and H+ antiporters, which are responsible for Na+ and H+ homeostasis in cells
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Functional and structural dynamics of NhaA, a prototype for Na+ and H+ antiporters, which are responsible for Na+ and H+ homeostasis in cells Functional and structural dynamics of NhaA, a prototype for Na+ and H+ antiporters, which are responsible for Na+ and H+ homeostasis in cells](/preview/png/10795659.png)
چکیده انگلیسی
The crystal structure of down-regulated NhaA crystallized at acidic pHÂ 4 [21] has provided the first structural insights into the antiport mechanism and pH regulation of a Na+/H+ antiporter [22]. On the basis of the NhaA crystal structure [21] and experimental data (reviewed in [2,22,38] we have suggested that NhaA is organized into two functional regions: (i) a cluster of amino acids responsible for pH regulation (ii) a catalytic region at the middle of the TM IV/XI assembly, with its unique antiparallel unfolded regions that cross each other forming a delicate electrostatic balance in the middle of the membrane. This unique structure contributes to the cation binding site and allows the rapid conformational changes expected for NhaA. Extended chains interrupting helices appear now a common feature for ion binding in transporters. However the NhaA fold is unique and shared by ASBTNM [30] and NapA [29]. Computation [13], electrophysiology [69] combined with biochemistry [33,47] have provided intriguing models for the mechanism of NhaA. However, the conformational changes and the residues involved have not yet been fully identified. Another issue which is still enigma is how energy is transduced “in this 'nano-machine.'” We expect that an integrative approach will reveal the residues that are crucial for NhaA activity and regulation, as well as elucidate the pHand ligand-induced conformational changes and their dynamics. Ultimately, integrative results will shed light on the mechanism of activity and pH regulation of NhaA, a prototype of the CPA2 family of transporters. This article is part of a Special Issue entitled: 18th European Bioenergetic Conference.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1837, Issue 7, July 2014, Pages 1047-1062
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1837, Issue 7, July 2014, Pages 1047-1062
نویسندگان
Etana Padan,