|
|
| (4 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Structure of thermophilic F1-ATPase inhibited by epsilon subunit== | | ==Structure of thermophilic F1-ATPase inhibited by epsilon subunit== |
| - | <StructureSection load='4xd7' size='340' side='right' caption='[[4xd7]], [[Resolution|resolution]] 3.90Å' scene=''> | + | <StructureSection load='4xd7' size='340' side='right'caption='[[4xd7]], [[Resolution|resolution]] 3.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xd7]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XD7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xd7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XD7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xd7 OCA], [https://pdbe.org/4xd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xd7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xd7 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xd7 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATPE_GEOKA ATPE_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] [[http://www.uniprot.org/uniprot/ATPA_GEOKA ATPA_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/ATPG_GEOKA ATPG_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. [[http://www.uniprot.org/uniprot/ATPB_GEOKA ATPB_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | + | [https://www.uniprot.org/uniprot/ATPA_BACP3 ATPA_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4xd7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: NAKASAKO, M]] | + | [[Category: Bacillus sp. PS3]] |
| - | [[Category: SHIRAKIHARA, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: SHIRATORI, A]] | + | [[Category: NAKASAKO M]] |
| - | [[Category: SUZUK, T]]
| + | [[Category: SHIRAKIHARA Y]] |
| - | [[Category: TANIKAWA, H]]
| + | [[Category: SHIRATORI A]] |
| - | [[Category: YOSHIDA, M]]
| + | [[Category: SUZUKI T]] |
| - | [[Category: Atp synthase]] | + | [[Category: TANIKAWA H]] |
| - | [[Category: Bacillus ps3]] | + | [[Category: YOSHIDA M]] |
| - | [[Category: F1-atpase]] | + | |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Rotary motor protein]] | + | |
| - | [[Category: Rotational catalysis]]
| + | |
| - | [[Category: Thermophilic]]
| + | |
| Structural highlights
Function
ATPA_BACP3 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346]
Publication Abstract from PubMed
F1 -ATPase (F1 ) is the catalytic sector in Fo F1 -ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic beta-subunits undergo nucleotide occupancy-dependent and concerted open-close conformational changes that are accompanied by rotation of the gamma-subunit. Bacterial and chloroplast F1 are inhibited by their own epsilon-subunit. In the epsilon-inhibited Escherichia coli F1 structure, the epsilon-subunit stabilizes the overall conformation (half-closed, closed, open) of the beta-subunits by inserting its C-terminal helix into the alpha3 beta3 cavity. The structure of epsilon-inhibited thermophilic F1 is similar to that of E. coli F1 , showing a similar conformation of the epsilon-subunit, but the thermophilic epsilon-subunit stabilizes another unique overall conformation (open, closed, open) of the beta-subunits. The epsilon-C-terminal helix 2 and hook are conserved between the two structures in interactions with target residues and in their positions. Rest of the epsilon-C-terminal domains are in quite different conformations and positions, and have different modes of interaction with targets. This region is thought to serve epsilon-inhibition differently. For inhibition, the epsilon-subunit contacts the second catches of some of the beta- and alpha-subunits, the N- and C-terminal helices, and some of the Rossmann fold segments. Those contacts, as a whole, lead to positioning of those beta- and alpha- second catches in epsilon-inhibition-specific positions, and prevent rotation of the gamma-subunit. Some of the structural features are observed even in IF1 inhibition in mitochondrial F1 . DATABASE: Structural data are available in the Worldwide Protein Data Bank database under the accession number 4XD7.
Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism.,Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M, Suzuki T FEBS J. 2015 Aug;282(15):2895-913. doi: 10.1111/febs.13329. Epub 2015 Jun 19. PMID:26032434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M, Suzuki T. Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism. FEBS J. 2015 Aug;282(15):2895-913. doi: 10.1111/febs.13329. Epub 2015 Jun 19. PMID:26032434 doi:http://dx.doi.org/10.1111/febs.13329
|
