1h8e
From Proteopedia
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| - | [[Image:1h8e.gif|left|200px]]<br /><applet load="1h8e" size=" | + | [[Image:1h8e.gif|left|200px]]<br /><applet load="1h8e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h8e, resolution 2.0Å" /> | caption="1h8e, resolution 2.0Å" /> | ||
'''(ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE (ALL THREE CATALYTIC SITES OCCUPIED)'''<br /> | '''(ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE (ALL THREE CATALYTIC SITES OCCUPIED)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H8E 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, ALF, SO4, ADP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=AC1:Adp Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Mg Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Adp Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:Mg Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:Adp Binding Site For Chain C'>AC5</scene>, <scene name='pdbsite=AC6:Mg Binding Site For Chain C'>AC6</scene>, <scene name='pdbsite=AC7:Adp Binding Site For Chain D'>AC7</scene>, <scene name='pdbsite=AC8:Mg Binding Site For Chain D'>AC8</scene>, <scene name='pdbsite=AC9:Alf Binding Site For Chain D'>AC9</scene>, <scene name='pdbsite=BC1:Adp Binding Site For Chain E'>BC1</scene>, <scene name='pdbsite=BC2:Mg Binding Site For Chain E'>BC2</scene>, <scene name='pdbsite=BC3:So4 Binding Site For Chain E'>BC3</scene>, <scene name='pdbsite=BC4:Adp Binding Site For Chain F'>BC4</scene>, <scene name='pdbsite=BC5:Mg Binding Site For Chain F'>BC5</scene>, <scene name='pdbsite=BC6:Alf Binding Site For Chain F'>BC6</scene>, <scene name='pdbsite=CAT:The Carboxylate Group Of GLU Residue Is Believed To Acti ...'>CAT</scene> and <scene name='pdbsite=PLP:LYS Within The P-Loop (Phosphate Bindi Motif, Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http:// | + | 1H8E 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Adp+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Adp+Binding+Site+For+Chain+C'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Chain+C'>AC6</scene>, <scene name='pdbsite=AC7:Adp+Binding+Site+For+Chain+D'>AC7</scene>, <scene name='pdbsite=AC8:Mg+Binding+Site+For+Chain+D'>AC8</scene>, <scene name='pdbsite=AC9:Alf+Binding+Site+For+Chain+D'>AC9</scene>, <scene name='pdbsite=BC1:Adp+Binding+Site+For+Chain+E'>BC1</scene>, <scene name='pdbsite=BC2:Mg+Binding+Site+For+Chain+E'>BC2</scene>, <scene name='pdbsite=BC3:So4+Binding+Site+For+Chain+E'>BC3</scene>, <scene name='pdbsite=BC4:Adp+Binding+Site+For+Chain+F'>BC4</scene>, <scene name='pdbsite=BC5:Mg+Binding+Site+For+Chain+F'>BC5</scene>, <scene name='pdbsite=BC6:Alf+Binding+Site+For+Chain+F'>BC6</scene>, <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Bindi+Motif,+Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:40 2008'' |
Revision as of 07:47, 3 February 2008
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(ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE (ALL THREE CATALYTIC SITES OCCUPIED)
Overview
The crystal structure of a novel aluminium fluoride inhibited form of, bovine mitochondrial F(1)-ATPase has been determined at 2 A resolution. In, contrast to all previously determined structures of the bovine enzyme, all, three catalytic sites are occupied by nucleotide. The subunit that did not, bind nucleotide in previous structures binds ADP and sulfate (mimicking, phosphate), and adopts a "half-closed" conformation. This structure, probably represents the posthydrolysis, pre-product release step on the, catalytic pathway. A catalytic scheme for hydrolysis (and synthesis) at, physiological rates and a mechanism for the ATP-driven rotation of the, gamma subunit are proposed based on the crystal structures of the bovine, enzyme.
About this Structure
1H8E is a Protein complex structure of sequences from Bos taurus with , , , and as ligands. 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
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis., Menz RI, Walker JE, Leslie AG, Cell. 2001 Aug 10;106(3):331-41. PMID:11509182
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