7wem
From Proteopedia
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==Solid-state NMR Structure of TFo c-Subunit Ring== | ==Solid-state NMR Structure of TFo c-Subunit Ring== | ||
| - | <StructureSection load='7wem' size='340' side='right'caption='[[7wem]]' scene=''> | + | <StructureSection load='7wem' size='340' side='right'caption='[[7wem]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7wem]] is a 10 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WEM FirstGlance]. <br> |
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7wem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wem OCA], [https://pdbe.org/7wem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wem RCSB], [https://www.ebi.ac.uk/pdbsum/7wem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wem ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7wem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wem OCA], [https://pdbe.org/7wem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wem RCSB], [https://www.ebi.ac.uk/pdbsum/7wem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wem ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/ATPL_BACP3 ATPL_BACP3]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Proton translocation through the membrane-embedded Fo component of F-type ATP synthase (FoF1) is facilitated by the rotation of the Fo c-subunit ring (c-ring), carrying protons at essential acidic amino acid residues. Cryo-electron microscopy (Cryo-EM) structures of FoF1 suggest a unique proton translocation mechanism. To elucidate it based on the chemical conformation of the essential acidic residues of the c-ring in FoF1, we determined the structure of the isolated thermophilic Bacillus Fo (tFo) c-ring, consisting of 10 subunits, in membranes by solid-state NMR. This structure contains a distinct proton-locking conformation, wherein Asn23 (cN23) C(gamma)O and Glu56 (cE56) C(delta)OH form a hydrogen bond in a closed form. We introduced stereo-array-isotope-labeled (SAIL) Glu and Asn into the tFoc-ring to clarify the chemical conformation of these residues in tFoF1-ATP synthase (tFoF1). Two well-separated (13)C signals could be detected for cN23 and cE56 in a 505 kDa membrane protein complex, respectively, thereby suggesting the presence of two distinct chemical conformations. Based on the signal intensity and structure of the tFoc-ring and tFoF1, six pairs of cN23 and cE56 surrounded by membrane lipids take the closed form, whereas the other four in the a-c interface employ the deprotonated open form at a proportion of 87%. This indicates that the a-c interface is highly hydrophilic. The pKa values of the four cE56 residues in the a-c interface were estimated from the cN23 signal intensity in the open and closed forms and distribution of polar residues around each cE56. The results favor a rotation of the c-ring for ATP synthesis. | ||
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| + | Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure.,Todokoro Y, Kang SJ, Suzuki T, Ikegami T, Kainosho M, Yoshida M, Fujiwara T, Akutsu H J Am Chem Soc. 2022 Jul 29. doi: 10.1021/jacs.2c03580. PMID:35905443<ref>PMID:35905443</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7wem" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Akutsu H]] | + | [[Category: Akutsu, H]] |
| - | [[Category: Fujiwara T]] | + | [[Category: Fujiwara, T]] |
| - | [[Category: Ikegami T]] | + | [[Category: Ikegami, T]] |
| - | [[Category: Kang S | + | [[Category: Kang, S J]] |
| - | [[Category: Suzuki T]] | + | [[Category: Suzuki, T]] |
| - | [[Category: Todokoro Y]] | + | [[Category: Todokoro, Y]] |
| - | [[Category: Yoshida M]] | + | [[Category: Yoshida, M]] |
| + | [[Category: Decamer helices ring in membrane atp synthase rotor]] | ||
| + | [[Category: Proton transport]] | ||
Revision as of 05:16, 25 August 2022
Solid-state NMR Structure of TFo c-Subunit Ring
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