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| | ==Crystal structure of subunit F of V-ATPase from S. cerevisiae== | | ==Crystal structure of subunit F of V-ATPase from S. cerevisiae== |
| - | <StructureSection load='4ix9' size='340' side='right' caption='[[4ix9]], [[Resolution|resolution]] 2.33Å' scene=''> | + | <StructureSection load='4ix9' size='340' side='right'caption='[[4ix9]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ix9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IX9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ix9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IX9 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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix9 OCA], [https://pdbe.org/4ix9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ix9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ix9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ix9 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VMA7, YGR020C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix9 OCA], [http://pdbe.org/4ix9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ix9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ix9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ix9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VATF_YEAST VATF_YEAST]] Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. | + | [https://www.uniprot.org/uniprot/VATF_YEAST VATF_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ix9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ix9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Balakrishna, A M]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Basak, S]] | + | [[Category: Balakrishna AM]] |
| - | [[Category: Gruber, G]] | + | [[Category: Basak S]] |
| - | [[Category: Manimekalai, M S.S]]
| + | [[Category: Gruber G]] |
| - | [[Category: Coupling]] | + | [[Category: Manimekalai MSS]] |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Regulatory]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Stalk subunit]]
| + | |
| - | [[Category: Subunit f]]
| + | |
| - | [[Category: V-atpase]]
| + | |
| Structural highlights
Function
VATF_YEAST Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Publication Abstract from PubMed
Subunit F of V-ATPases is proposed to undergo structural alterations during catalysis and reversible dissociation from the V1VO complex. Recently, we determined the low resolution structure of F from Saccharomyces cerevisiae V-ATPase, showing an N-terminal egg shape, connected to a C-terminal hook-like segment via a linker region. To understand the mechanistic role of subunit F of S. cerevisiae V-ATPase, composed of 118 amino acids, the crystal structure of the major part of F, F(1-94), was solved at 2.3 A resolution. The structural features were confirmed by solution NMR spectroscopy using the entire F subunit. The eukaryotic F subunit consists of the N-terminal F(1-94) domain with four-parallel beta-strands, which are intermittently surrounded by four alpha-helices, and the C terminus, including the alpha5-helix encompassing residues 103 to 113. Two loops (26)GQITPETQEK(35) and (60)ERDDI(64) are described to be essential in mechanistic processes of the V-ATPase enzyme. The (26)GQITPETQEK(35) loop becomes exposed when fitted into the recently determined EM structure of the yeast V1VO-ATPase. A mechanism is proposed in which the (26)GQITPETQEK(35) loop of subunit F and the flexible C-terminal domain of subunit H move in proximity, leading to an inhibitory effect of ATPase activity in V1. Subunits D and F are demonstrated to interact with subunit d. Together with NMR dynamics, the role of subunit F has been discussed in the light of its interactions in the processes of reversible disassembly and ATP hydrolysis of V-ATPases by transmitting movements of subunit d and H of the VO and V1 sector, respectively.
Crystal and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae.,Basak S, Lim J, Manimekalai MS, Balakrishna AM, Gruber G J Biol Chem. 2013 Apr 26;288(17):11930-9. doi: 10.1074/jbc.M113.461533. Epub 2013, Mar 8. PMID:23476018[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Basak S, Lim J, Manimekalai MS, Balakrishna AM, Gruber G. Crystal and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J Biol Chem. 2013 Apr 26;288(17):11930-9. doi: 10.1074/jbc.M113.461533. Epub 2013, Mar 8. PMID:23476018 doi:10.1074/jbc.M113.461533
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