1fs0
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(New page: 200px<br /><applet load="1fs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fs0, resolution 2.1Å" /> '''COMPLEX OF GAMMA/EPSI...)
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Revision as of 13:05, 20 November 2007
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COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI
Overview
ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of, protons down a transmembrane electrochemical gradient to drive the, synthesis of ATP, the universal biological energy currency. Proton flow, through F(o) drives rotation of a ring of c-subunits and a complex of the, gamma and epsilon-subunits, causing cyclical conformational changes in, F(1) that are required for catalysis. The crystal structure of a large, portion of F(1) has been resolved. However, the structure of the central, portion of the enzyme, through which conformational changes in F(o) are, communicated to F(1), has until now remained elusive. Here we report the, crystal structure of a complex of the epsilon-subunit and the central, domain of the gamma-subunit refined at 2.1 A resolution. The structure, reveals how rotation of these subunits causes large conformational changes, in F(1), and thereby provides new insights into energy coupling between, F(o) and F(1).
About this Structure
1FS0 is a Protein complex structure of sequences from Escherichia coli. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Structure of the gamma-epsilon complex of ATP synthase., Rodgers AJ, Wilce MC, Nat Struct Biol. 2000 Nov;7(11):1051-4. PMID:11062562
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