From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1sky.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1sky.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1sky| PDB=1sky | SCENE= }} | | {{STRUCTURE_1sky| PDB=1sky | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3'''
| + | ===CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | BACKGROUND: F1-ATPase, an oligomeric assembly with subunit stoichiometry alpha 3 beta 3 gamma delta epsilon, is the catalytic component of the ATP synthase complex, which plays a central role in energy transduction in bacteria, chloroplasts and mitochondria. The crystal structure of bovine mitochondrial F1-ATPase displays a marked asymmetry in the conformation and nucleotide content of the catalytic beta subunits. The alpha 3 beta 3 subcomplex of F1-ATPase has been assembled from subunits of the moderately thermophilic Bacillus PS3 made in Escherichia coli, and the subcomplex is active but does not show the catalytic cooperativity of intact F1-ATPase. The structure of this subcomplex should provide new information on the conformational variability of F1-ATPase and may provide insights into the unusual catalytic mechanism employed by this enzyme. RESULTS: The crystal structure of the nucleotide-free bacterial alpha 3 beta 3 subcomplex of F1-ATPase, determined at 3.2 A resolution, shows that the oligomer has exact threefold symmetry. The bacterial beta subunits adopt a conformation essentially identical to that of the nucleotide-free beta subunit in mitochondrial F1-ATPase; the alpha subunits have similar conformations in both structures. CONCLUSIONS: The structures of the bacterial F1-ATPase alpha and beta subunits are very similar to their counterparts in the mitochondrial enzyme, suggesting a common catalytic mechanism. The study presented here allows an analysis of the different conformations adopted by the alpha and beta subunits and may ultimately further our understanding of this mechanism.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9261073}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9261073 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9261073}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 37: |
Line 41: |
| | [[Category: F1fo atp synthase]] | | [[Category: F1fo atp synthase]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:49:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:11:43 2008'' |
Revision as of 04:11, 28 July 2008
Template:STRUCTURE 1sky
CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3
Template:ABSTRACT PUBMED 9261073
About this Structure
1SKY is a Protein complex structure of sequences from Bacillus sp. ps3. Full crystallographic information is available from OCA.
Reference
The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer., Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T, Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M, Structure. 1997 Jun 15;5(6):825-36. PMID:9261073
Page seeded by OCA on Mon Jul 28 07:11:43 2008
Categories: Bacillus sp. ps3 | Protein complex | Abrahams, J P. | Kagawa, Y. | Kambara, M. | Leslie, A G.W. | Saika, K. | Sekimoto, Y. | Shirakihara, Y. | Ueda, T. | Walker, J E. | Yoshida, M. | Alpha3beta3 subcomplex of f1-atpase | Atp synthase | F1-atpase | F1fo atp synthase | Hydrolase
