|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Structure at 2.3 A of the alpha/beta monomer of the F-ATPase from Paracoccus denitrificans== | | ==Structure at 2.3 A of the alpha/beta monomer of the F-ATPase from Paracoccus denitrificans== |
| - | <StructureSection load='5cdf' size='340' side='right' caption='[[5cdf]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5cdf' size='340' side='right'caption='[[5cdf]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cdf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CDF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cdf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CDF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5cdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cdf OCA], [http://pdbe.org/5cdf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cdf RCSB], [http://www.ebi.ac.uk/pdbsum/5cdf PDBsum]</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=5cdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cdf OCA], [https://pdbe.org/5cdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cdf RCSB], [https://www.ebi.ac.uk/pdbsum/5cdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cdf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATPA_PARDP ATPA_PARDP]] 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/ATPB_PARDP ATPB_PARDP]] 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_PARDP ATPA_PARDP] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5cdf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5cdf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Paracoccus denitrificans]] | | [[Category: Paracoccus denitrificans]] |
| - | [[Category: Garcia-Trejo, J J]] | + | [[Category: Garcia-Trejo JJ]] |
| - | [[Category: Leslie, A G.W]] | + | [[Category: Leslie AGW]] |
| - | [[Category: Montgomery, M G]] | + | [[Category: Montgomery MG]] |
| - | [[Category: Morales-Rios, E]] | + | [[Category: Morales-Rios E]] |
| - | [[Category: Walker, J E]] | + | [[Category: Walker JE]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
ATPA_PARDP Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Publication Abstract from PubMed
The structures of F-ATPases have predominantly been determined from mitochondrial enzymes, and those of the enzymes in eubacteria have been less studied. Paracoccus denitrificans is a member of the alpha-proteobacteria and is related to the extinct protomitochondrion that became engulfed by the ancestor of eukaryotic cells. The P. denitrificans F-ATPase is an example of a eubacterial F-ATPase that can carry out ATP synthesis only, whereas many others can catalyse both the synthesis and the hydrolysis of ATP. Inhibition of the ATP hydrolytic activity of the P. denitrificans F-ATPase involves the zeta inhibitor protein, an alpha-helical protein that binds to the catalytic F1 domain of the enzyme. This domain is a complex of three alpha-subunits and three beta-subunits, and one copy of each of the gamma-, delta- and -subunits. Attempts to crystallize the F1-zeta inhibitor complex yielded crystals of a subcomplex of the catalytic domain containing the alpha- and beta-subunits only. Its structure was determined to 2.3 A resolution and consists of a heterodimer of one alpha-subunit and one beta-subunit. It has no bound nucleotides, and it corresponds to the `open' or `empty' catalytic interface found in other F-ATPases. The main significance of this structure is that it aids in the determination of the structure of the intact membrane-bound F-ATPase, which has been crystallized.
Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 A resolution.,Morales-Rios E, Montgomery MG, Leslie AG, Garcia-Trejo JJ, Walker JE Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1309-17. doi:, 10.1107/S2053230X15016076. Epub 2015 Sep 23. PMID:26457523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morales-Rios E, Montgomery MG, Leslie AG, Garcia-Trejo JJ, Walker JE. Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 A resolution. Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1309-17. doi:, 10.1107/S2053230X15016076. Epub 2015 Sep 23. PMID:26457523 doi:http://dx.doi.org/10.1107/S2053230X15016076
|
