1nbm
From Proteopedia
| Line 4: | Line 4: | ||
|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= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TYN:AMINOBENZOFURAZAN-O-TYROSINE'>TYN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbm OCA], [http://www.ebi.ac.uk/pdbsum/1nbm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nbm RCSB]</span> | ||
}} | }} | ||
| Line 21: | Line 24: | ||
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] | 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: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Transferred entry: 3 6.3 14]] | ||
[[Category: Braig, K.]] | [[Category: Braig, K.]] | ||
[[Category: Leslie, A G.W.]] | [[Category: Leslie, A G.W.]] | ||
[[Category: Orriss, G L.]] | [[Category: Orriss, G L.]] | ||
[[Category: Walker, J E.]] | [[Category: Walker, J E.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PO4]] | ||
[[Category: 4-chloro-7-nitrobenzofurazan]] | [[Category: 4-chloro-7-nitrobenzofurazan]] | ||
[[Category: atp synthase]] | [[Category: atp synthase]] | ||
| Line 37: | Line 36: | ||
[[Category: inhibition]] | [[Category: inhibition]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:06 2008'' |
Revision as of 19:28, 30 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , , , | ||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 30 22:28:06 2008
