Academic Journal
Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation
| العنوان: | Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation |
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| المؤلفون: | Symersky, J, Pagadala, V, Osowski, D, Krah, A, Meier, T, Faraldo-Gomez, JD, Mueller, DM |
| المصدر: | 491 ; 485 |
| بيانات النشر: | Nature Research |
| سنة النشر: | 2012 |
| المجموعة: | Imperial College London: Spiral |
| مصطلحات موضوعية: | Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Biophysics, Cell Biology, TRANSFER-RNA TRANSFORMYLASE, BOVINE HEART-MITOCHONDRIA, SUBUNIT-C, ROTOR RING, PROTON TRANSLOCATION, MEMBRANE-PROTEINS, NA+-ATPASE, BINDING, MECHANISM, REGION, Binding Sites, Crystallography, X-Ray, Mitochondrial Proton-Translocating ATPases, Molecular Dynamics Simulation, Protein Conformation, Protein Subunits, Protons, Saccharomyces cerevisiae, Developmental Biology |
| الوصف: | The proton pore of the F1Fo ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1545-9985 |
| Relation: | Nature Structural and Molecular Biology; http://hdl.handle.net/10044/1/94603 |
| DOI: | 10.1038/nsmb.2284 |
| الاتاحة: | http://hdl.handle.net/10044/1/94603 https://doi.org/10.1038/nsmb.2284 |
| Rights: | © 2012 Nature America, Inc. All rights reserved. |
| رقم الانضمام: | edsbas.6669E58 |
| قاعدة البيانات: | BASE |
| تدمد: | 15459985 |
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| DOI: | 10.1038/nsmb.2284 |