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5ik2
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5ik2 is ON HOLD Authors: Ferguson, S.A., Cook, G.M., Montgomery, M.G., Leslie, A.G.W., Walker, J.E. Description: Caldalaklibacillus thermarum F1-AT...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Caldalaklibacillus thermarum F1-ATPase (epsilon mutant)== | |
| + | <StructureSection load='5ik2' size='340' side='right'caption='[[5ik2]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ik2]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldalkalibacillus_thermarum_TA2.A1 Caldalkalibacillus thermarum TA2.A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IK2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ik2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ik2 OCA], [https://pdbe.org/5ik2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ik2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ik2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ik2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F5LA73_CALTT F5LA73_CALTT] 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.[ARBA:ARBA00003456][HAMAP-Rule:MF_00815] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure has been determined of the F1-catalytic domain of the F-ATPase from Caldalkalibacillus thermarum, which hydrolyzes adenosine triphosphate (ATP) poorly. It is very similar to those of active mitochondrial and bacterial F1-ATPases. In the F-ATPase from Geobacillus stearothermophilus, conformational changes in the epsilon-subunit are influenced by intracellular ATP concentration and membrane potential. When ATP is plentiful, the epsilon-subunit assumes a "down" state, with an ATP molecule bound to its two C-terminal alpha-helices; when ATP is scarce, the alpha-helices are proposed to inhibit ATP hydrolysis by assuming an "up" state, where the alpha-helices, devoid of ATP, enter the alpha3beta3-catalytic region. However, in the Escherichia coli enzyme, there is no evidence that such ATP binding to the epsilon-subunit is mechanistically important for modulating the enzyme's hydrolytic activity. In the structure of the F1-ATPase from C. thermarum, ATP and a magnesium ion are bound to the alpha-helices in the down state. In a form with a mutated epsilon-subunit unable to bind ATP, the enzyme remains inactive and the epsilon-subunit is down. Therefore, neither the gamma-subunit nor the regulatory ATP bound to the epsilon-subunit is involved in the inhibitory mechanism of this particular enzyme. The structure of the alpha3beta3-catalytic domain is likewise closely similar to those of active F1-ATPases. However, although the betaE-catalytic site is in the usual "open" conformation, it is occupied by the unique combination of an ADP molecule with no magnesium ion and a phosphate ion. These bound hydrolytic products are likely to be the basis of inhibition of ATP hydrolysis. | ||
| - | + | Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.,Ferguson SA, Cook GM, Montgomery MG, Leslie AG, Walker JE Proc Natl Acad Sci U S A. 2016 Sep 27;113(39):10860-5. doi:, 10.1073/pnas.1612035113. Epub 2016 Sep 12. PMID:27621435<ref>PMID:27621435</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ik2" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Caldalkalibacillus thermarum TA2 A1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cook GM]] | ||
| + | [[Category: Ferguson SA]] | ||
| + | [[Category: Leslie AGW]] | ||
| + | [[Category: Montgomery MG]] | ||
| + | [[Category: Walker JE]] | ||
Current revision
Caldalaklibacillus thermarum F1-ATPase (epsilon mutant)
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