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1nbm
From Proteopedia
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|PDB= 1nbm |SIZE=350|CAPTION= <scene name='initialview01'>1nbm</scene>, resolution 3.0Å | |PDB= 1nbm |SIZE=350|CAPTION= <scene name='initialview01'>1nbm</scene>, resolution 3.0Å | ||
|SITE= <scene name='pdbsite=CA1:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA1</scene>, <scene name='pdbsite=CA2:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA2</scene>, <scene name='pdbsite=CA3:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA3</scene>, <scene name='pdbsite=PL1:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL1</scene>, <scene name='pdbsite=PL2:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL2</scene>, <scene name='pdbsite=PL3:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL3</scene>, <scene name='pdbsite=PL4:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL4</scene>, <scene name='pdbsite=PL5:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL5</scene>, <scene name='pdbsite=PL6:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL6</scene> and <scene name='pdbsite=PL7:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL7</scene> | |SITE= <scene name='pdbsite=CA1:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA1</scene>, <scene name='pdbsite=CA2:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA2</scene>, <scene name='pdbsite=CA3:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CA3</scene>, <scene name='pdbsite=PL1:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL1</scene>, <scene name='pdbsite=PL2:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL2</scene>, <scene name='pdbsite=PL3:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL3</scene>, <scene name='pdbsite=PL4:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL4</scene>, <scene name='pdbsite=PL5:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL5</scene>, <scene name='pdbsite=PL6:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL6</scene> and <scene name='pdbsite=PL7:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PL7</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</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: inhibition]] | [[Category: inhibition]] | ||
| - | ''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 12:52:53 2008'' |
Revision as of 10:52, 23 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Transferred entry: 3.6.3.14, with EC number 3.6.1.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
Overview
BACKGROUND: F1-ATPase is the globular domain of F1F0-ATP synthase that catalyses the hydrolysis of ATP to ADP and phosphate. The crystal structure of bovine F1-ATPase has been determined previously to 2.8 A resolution. The enzyme comprises five different subunits in the stoichiometry alpha 3 beta 3 gamma delta epsilon; the three catalytic beta subunits alternate with the three alpha subunits around the centrally located single gamma subunit. To understand more about the catalytic mechanisms, F1-ATPase was inhibited by reaction with 4-chloro-7-nitrobenzofurazan (NBD-Cl) and the structure of the inhibited complex (F1-NBD) determined by X-ray crystallography. RESULTS: In the structure the three beta subunits adopt a different conformation with different nucleotide occupancy. NBD-Cl reacts with the phenolic oxygen of Tyr311 of the beta E subunit, which contains no bound nucleotide. The two other catalytic subunits beta TP and beta DP contain bound adenylyl-imidodiphosphate (AMP-PNP) and ADP, respectively. The binding site of the NBD moiety does not overlap with the regions of beta E that form the nucleotide-binding pocket in subunits beta TP and beta DP nor does it occlude the nucleotide-binding site. Catalysis appears to be inhibited because neither beta TP nor beta DP can accommodate a Tyr311 residue bearing an NBD group. CONCLUSIONS: The results presented here are consistent with a rotary catalytic mechanism of ATP synthesis and hydrolysis, which requires the sequential and concerted participation of all three catalytic sites. NBD-Cl inhibits the enzyme by preventing the modified subunit from adopting a conformation that is essential for catalysis to proceed.
About this Structure
1NBM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism., Orriss GL, Leslie AG, Braig K, Walker JE, Structure. 1998 Jul 15;6(7):831-7. PMID:9687365
Page seeded by OCA on Sun Mar 23 12:52:53 2008
