1e79: Difference between revisions

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[[Image:1e79.~~gif~~|left|200px]]

[[Image:1e79.png|left|200px]]

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~~==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) domain.

==About this Structure==

1E79 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E79 OCA].

~~==Reference==~~

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:[http://www.ncbi.nlm.nih.gov/pubmed/11062563 11062563]

[[Category: ATP Synthase]]

[[Category: Bos taurus]]

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[[Category: F1-atpase]]

[[Category: F1fo atp synthase]]

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-[[Image:1e79.gif|left|200px]]
+[[Image:1e79.png|left|200px]]
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-==Overview==
+{{ABSTRACT_11062563}}
-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==
 E79 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E79 OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11062563 11062563]
 [[Category: ATP Synthase]]
 [[Category: Bos taurus]]
@@ Line 34: / Line 30: @@
 [[Category: F1-atpase]]
 [[Category: F1fo atp synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:45:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:12:38 2008''