1e79: Difference between revisions
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==Overview== | ==Overview== | ||
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) . | 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) domain. | ||
==About this Structure== | ==About this Structure== | ||
1E79 is a | 1E79 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, SO4, ATP, ADP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1E79 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb72_1.html ATP Synthase]]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] Structure known Active Sites: AT1, AT2, AT3, AT4, AT5, CAT and PLP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E79 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
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Revision as of 13:52, 5 November 2007
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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) domain.
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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