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.
4mjn
From Proteopedia
Contents |
Structure of the c ring of the CF1FO ATP synthases.
Template:ABSTRACT PUBMED 24521269
Function
[ATPH_WHEAT] 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 (By similarity). Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).
About this Structure
4mjn is a 14 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
- Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G. Crystallographic structure of the turbine c-ring from spinach chloroplast F-ATP synthase. Biosci Rep. 2014 Feb 13. PMID:24521269 doi:http://dx.doi.org/10.1042/BSR20130114
