1e79: Difference between revisions
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|PDB= 1e79 |SIZE=350|CAPTION= <scene name='initialview01'>1e79</scene>, resolution 2.4Å | |PDB= 1e79 |SIZE=350|CAPTION= <scene name='initialview01'>1e79</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=AT1:Atp+Binding+Site+For+Chain+A'>AT1</scene>, <scene name='pdbsite=AT2:Adp+Binding+Site+For+Chain+B'>AT2</scene>, <scene name='pdbsite=AT3:Atp+Binding+Site+For+Chain+C'>AT3</scene>, <scene name='pdbsite=AT4:Adp+Binding+Site+For+Chain+D'>AT4</scene>, <scene name='pdbsite=AT5:Adp+Binding+Site+For+Chain+F'>AT5</scene>, <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+Glutamic+Aci+Residue+Is+Believe+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene> | |SITE= <scene name='pdbsite=AT1:Atp+Binding+Site+For+Chain+A'>AT1</scene>, <scene name='pdbsite=AT2:Adp+Binding+Site+For+Chain+B'>AT2</scene>, <scene name='pdbsite=AT3:Atp+Binding+Site+For+Chain+C'>AT3</scene>, <scene name='pdbsite=AT4:Adp+Binding+Site+For+Chain+D'>AT4</scene>, <scene name='pdbsite=AT5:Adp+Binding+Site+For+Chain+F'>AT5</scene>, <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+Glutamic+Aci+Residue+Is+Believe+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene> | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= [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] | ||
|GENE= | |GENE= | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:36:56 2008'' | ||
Revision as of 12:36, 23 March 2008
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| , resolution 2.4Å | |||||||
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| Sites: | , , , , , and | ||||||
| Ligands: | , , , and | ||||||
| Activity: | Transferred entry: 3.6.3.14, with EC number 3.6.1.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. The following page contains interesting information on the relation of 1E79 with [ATP Synthase]. 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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