6f36: Difference between revisions
m Protected "6f36" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Polytomella Fo model== | |||
<StructureSection load='6f36' size='340' side='right' caption='[[6f36]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f36]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Polytomella_sp._pringsheim_198.80 Polytomella sp. pringsheim 198.80]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F36 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f36 OCA], [http://pdbe.org/6f36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f36 RCSB], [http://www.ebi.ac.uk/pdbsum/6f36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f36 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ATP synthases produce ATP by rotary catalysis, powered by the electrochemical proton gradient across the membrane. Understanding this fundamental process requires an atomic model of the proton pathway. We determined the structure of an intact mitochondrial ATP synthase dimer by electron cryo-microscopy at near-atomic resolution. Charged and polar residues of the a-subunit stator define two aqueous channels, each spanning one half of the membrane. Passing through a conserved membrane-intrinsic helix hairpin, the lumenal channel protonates an acidic glutamate in the c-ring rotor. Upon ring rotation, the protonated glutamate encounters the matrix channel and deprotonates. An arginine between the two channels prevents proton leakage. The steep potential gradient over the sub-nm inter-channel distance exerts a force on the deprotonated glutamate, resulting in net directional rotation. | |||
Structural basis of proton translocation and force generation in mitochondrial ATP synthase.,Klusch N, Murphy BJ, Mills DJ, Yildiz O, Kuhlbrandt W Elife. 2017 Dec 6;6. doi: 10.7554/eLife.33274. PMID:29210357<ref>PMID:29210357</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6f36" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Polytomella sp. pringsheim 198 80]] | |||
[[Category: Klusch, N]] | |||
[[Category: Kuehlbrandt, W]] | |||
[[Category: Mills, D J]] | |||
[[Category: Murphy, B J]] | |||
[[Category: Yildiz, O]] | |||
[[Category: Electron cryo-microscopy mitochondrial atp synthase membrane protein energy conversion proton pathway]] | |||
[[Category: Proton transport]] | |||