This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7wem
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | 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
| |||||||||||
