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| | <StructureSection load='2r31' size='340' side='right'caption='[[2r31]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='2r31' size='340' side='right'caption='[[2r31]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2r31]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pardp Pardp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R31 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2r31]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R31 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p4x|2p4x]], [[2p4f|2p4f]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDEN_0792 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</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=2r31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r31 OCA], [https://pdbe.org/2r31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r31 RCSB], [https://www.ebi.ac.uk/pdbsum/2r31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r31 ProSAT]</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=2r31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r31 OCA], [https://pdbe.org/2r31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r31 RCSB], [https://www.ebi.ac.uk/pdbsum/2r31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r31 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A1B060_PARDP A1B060_PARDP] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pardp]] | + | [[Category: Paracoccus denitrificans PD1222]] |
| - | [[Category: Ackerman, S H]] | + | [[Category: Ackerman SH]] |
| - | [[Category: Brunzelle, J S]] | + | [[Category: Brunzelle JS]] |
| - | [[Category: Gatti, D L]] | + | [[Category: Gatti DL]] |
| - | [[Category: Ludlam, A V]] | + | [[Category: Ludlam AV]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Chaperone f1 atpase assembly atp12p]]
| + | |
| Structural highlights
Function
A1B060_PARDP
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mitochondrial F(1)-ATPase contains a hexamer of alternating alpha and beta subunits. The assembly of this structure requires two specialized chaperones, Atp11p and Atp12p, that bind transiently to beta and alpha. In the absence of Atp11p and Atp12p, the hexamer is not formed, and alpha and beta precipitate as large insoluble aggregates. An early model for the mechanism of chaperone-mediated F(1) assembly (Wang, Z. G., Sheluho, D., Gatti, D. L., and Ackerman, S. H. (2000) EMBO J. 19, 1486-1493) hypothesized that the chaperones themselves look very much like the alpha and beta subunits, and proposed an exchange of Atp11p for alpha and of Atp12p for beta; the driving force for the exchange was expected to be a higher affinity of alpha and beta for each other than for the respective chaperone partners. One important feature of this model was the prediction that as long as Atp11p is bound to beta and Atp12p is bound to alpha, the two F(1) subunits cannot interact at either the catalytic site or the noncatalytic site interface. Here we present the structures of Atp11p from Candida glabrata and Atp12p from Paracoccus denitrificans, and we show that some features of the Wang model are correct, namely that binding of the chaperones to alpha and beta prevents further interactions between these F(1) subunits. However, Atp11p and Atp12p do not resemble alpha or beta, and it is instead the F(1) gamma subunit that initiates the release of the chaperones from alpha and beta and their further assembly into the mature complex.
Chaperones of F1-ATPase.,Ludlam A, Brunzelle J, Pribyl T, Xu X, Gatti DL, Ackerman SH J Biol Chem. 2009 Jun 19;284(25):17138-46. Epub 2009 Apr 21. PMID:19383603[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ludlam A, Brunzelle J, Pribyl T, Xu X, Gatti DL, Ackerman SH. Chaperones of F1-ATPase. J Biol Chem. 2009 Jun 19;284(25):17138-46. Epub 2009 Apr 21. PMID:19383603 doi:10.1074/jbc.M109.002568
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