1e1q
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1e1q.jpg|left|200px]]<br /><applet load="1e1q" size=" | + | [[Image:1e1q.jpg|left|200px]]<br /><applet load="1e1q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e1q, resolution 2.61Å" /> | caption="1e1q, resolution 2.61Å" /> | ||
'''BOVINE MITOCHONDRIAL F1-ATPASE AT 100K'''<br /> | '''BOVINE MITOCHONDRIAL F1-ATPASE AT 100K'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1E1Q 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, PO4, ANP and ADP 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=CAT:The Carboxylate Group Of GLU Residue Is Believed To Acti ...'>CAT</scene> and <scene name='pdbsite=PLP:LYS Within The P-Loop (Phosphate Binding) Motif, Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http:// | + | 1E1Q 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=PO4:'>PO4</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=ADP:'>ADP</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=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1Q OCA]. |
==Reference== | ==Reference== | ||
| Line 29: | Line 29: | ||
[[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 09:36:39 2008'' |
Revision as of 07:36, 3 February 2008
|
BOVINE MITOCHONDRIAL F1-ATPASE AT 100K
Overview
BACKGROUND: The globular domain of the membrane-associated F(1)F(o)-ATP, synthase complex can be detached intact as a water-soluble fragment known, as F(1)-ATPase. It consists of five different subunits, alpha, beta, gamma, delta and epsilon, assembled with the stoichiometry 3:3:1:1:1. In, the crystal structure of bovine F(1)-ATPase determined previously at 2.8 A, resolution, the three catalytic beta subunits and the three noncatalytic, alpha subunits are arranged alternately around a central alpha-helical, coiled coil in the gamma subunit. In the crystals, the catalytic sites, have different nucleotide occupancies. One contains the triphosphate form, of the nucleotide, the second contains the diphosphate, and the third is, unoccupied. Fluoroaluminate complexes have been shown to mimic the, transition state in several ATP and GTP hydrolases. In order to understand, more about its catalytic mechanism, F(1)-ATPase was inhibited with, Mg(2+)ADP and aluminium fluoride and the structure of the inhibited, complex was determined by X-ray crystallography. RESULTS: The structure of, bovine F(1)-ATPase inhibited with Mg(2+)ADP and aluminium fluoride, determined at 2.5 A resolution differs little from the original structure, with bound AMP-PNP and ADP. The nucleotide occupancies of the alpha and, beta subunits are unchanged except that both aluminium trifluoride and, Mg(2+)ADP are bound in the nucleotide-binding site of the beta(DP), subunit. The presence of aluminium fluoride is accompanied by only minor, adjustments in the surrounding protein. CONCLUSIONS: The structure appears, to mimic a possible transition state. The coordination of the, aluminofluoride group has many features in common with other, aluminofluoride-NTP hydrolase complexes. Apparently, once nucleotide is, bound to the catalytic beta subunit, no additional major structural, changes are required for catalysis to occur.
About this Structure
1E1Q 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 inhibited by Mg(2+) ADP and aluminium fluoride., Braig K, Menz RI, Montgomery MG, Leslie AG, Walker JE, Structure. 2000 Jun 15;8(6):567-73. PMID:10873854
Page seeded by OCA on Sun Feb 3 09:36:39 2008
