1e79

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==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) domain.
+
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==
Line 14: Line 14:
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Transferred entry: 3.6.3.14]]
+
[[Category: Transferred entry: 3 6.3 14]]
[[Category: Gibbons, C.]]
[[Category: Gibbons, C.]]
-
[[Category: Leslie, A.G.W.]]
+
[[Category: Leslie, A G.W.]]
-
[[Category: Montgomery, M.G.]]
+
[[Category: Montgomery, M G.]]
-
[[Category: Walker, J.E.]]
+
[[Category: Walker, J E.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: ATP]]
[[Category: ATP]]
Line 33: Line 33:
[[Category: f1fo atp synthase]]
[[Category: f1fo atp synthase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:37:54 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:37 2008''

Revision as of 10:24, 21 February 2008


1e79, resolution 2.4Å

Drag the structure with the mouse to rotate

BOVINE F1-ATPASE INHIBITED BY DCCD (DICYCLOHEXYLCARBODIIMIDE)

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 Bos taurus with , , , and 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 Known structural/functional Sites: , , , , , and . Full crystallographic information is available from 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:11062563

Page seeded by OCA on Thu Feb 21 12:24:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools