1e79: Difference between revisions

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[[Category: f1fo atp synthase]]
[[Category: f1fo atp synthase]]


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Revision as of 16:02, 30 October 2007

File:1e79.gif


1e79, resolution 2.4Å

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BOVINE F1-ATPASE INHIBITED BY DCCD (DICYCLOHEXYLCARBODIIMIDE)

OverviewOverview

The central stalk in ATP synthase, made of gamma, delta and epsilon, subunits in the mitochondrial enzyme, is the key rotary element in the, enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic, (alpha beta)(3) domain and protrudes beneath it, interacting with a ring, of c subunits in the membrane that drives rotation of the stalk during ATP, synthesis. In other crystals of F(1)-ATPase, the protrusion was, disordered, but with crystals of F(1)-ATPase inhibited with, dicyclohexylcarbodiimide, the complete structure was revealed. The delta, and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and, couples the transmembrane proton motive force to catalysis in the (alpha, beta)(3) ... [(full description)]

About this StructureAbout this Structure

1E79 is a [Protein complex] structure of sequences from [Bos taurus] with MG, SO4, ATP, ADP and GOL as [ligands]. The following page contains interesting information on the relation of 1E79 with [ATP Synthase]. Active as [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: AT1, AT2, AT3, AT4, AT5, CAT and PLP. Full crystallographic information is available from [OCA].

ReferenceReference

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution., Gibbons C, Montgomery MG, Leslie AG, Walker JE, Nat Struct Biol. 2000 Nov;7(11):1055-61. PMID:11062563

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OCA