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| | {{STRUCTURE_1nbm| PDB=1nbm | SCENE= }} | | {{STRUCTURE_1nbm| PDB=1nbm | SCENE= }} |
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| - | '''THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN'''
| + | ===THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9687365}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9687365 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9687365}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: F1fo atp synthase]] | | [[Category: F1fo atp synthase]] |
| | [[Category: Inhibition]] | | [[Category: Inhibition]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:20:14 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:47:33 2008'' |
Revision as of 08:47, 28 July 2008
Template:STRUCTURE 1nbm
THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
Template:ABSTRACT PUBMED 9687365
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 Mon Jul 28 11:47:33 2008
