Academic Journal
Crystal structure of yeast V 1 ‐ ATPase in the autoinhibited state
| العنوان: | Crystal structure of yeast V 1 ‐ ATPase in the autoinhibited state |
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| المؤلفون: | Oot, Rebecca A, Kane, Patricia M, Berry, Edward A, Wilkens, Stephan |
| المساهمون: | National Science Foundation, National Institute of General Medical Sciences, National Institutes of Health |
| المصدر: | The EMBO Journal ; volume 35, issue 15, page 1694-1706 ; ISSN 0261-4189 1460-2075 |
| بيانات النشر: | Springer Science and Business Media LLC |
| سنة النشر: | 2016 |
| الوصف: | Vacuolar ATP ases (V‐ ATP ases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V‐ ATP ase activity is regulated by a unique mechanism referred to as reversible disassembly, wherein the soluble catalytic sector, V 1 , is released from the membrane and its Mg ATP ase activity silenced. The crystal structure of yeast V 1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C‐terminal domain rotating ~150° from a position near the membrane in holo V‐ ATP ase to a position at the bottom of V 1 near an open catalytic site. Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATP ase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.15252/embj.201593447 |
| الاتاحة: | http://dx.doi.org/10.15252/embj.201593447 https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201593447 https://onlinelibrary.wiley.com/doi/full-xml/10.15252/embj.201593447 https://www.embopress.org/doi/am-pdf/10.15252/embj.201593447 https://www.embopress.org/doi/pdf/10.15252/embj.201593447 |
| Rights: | http://onlinelibrary.wiley.com/termsAndConditions#am ; http://onlinelibrary.wiley.com/termsAndConditions#vor |
| رقم الانضمام: | edsbas.47AFF21A |
| قاعدة البيانات: | BASE |
| DOI: | 10.15252/embj.201593447 |
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