1nbm: Difference between revisions
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'''THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN''' | {{Structure | ||
|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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NBM is a [ | 1NBM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9687365 9687365] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: inhibition]] | [[Category: inhibition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:45 2008'' | ||
Revision as of 13:54, 20 March 2008
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| , resolution 3.0Å | |||||||
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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 | ||||||
THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
OverviewOverview
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 StructureAbout this Structure
1NBM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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
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