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| | ==Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.== | | ==Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.== |
| - | <StructureSection load='4rnd' size='340' side='right' caption='[[4rnd]], [[Resolution|resolution]] 3.18Å' scene=''> | + | <StructureSection load='4rnd' size='340' side='right'caption='[[4rnd]], [[Resolution|resolution]] 3.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rnd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RND FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rnd]] 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=4RND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RND 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></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]] 3.18Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ix9|4ix9]]</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></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=4rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rnd RCSB], [http://www.ebi.ac.uk/pdbsum/4rnd 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=4rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnd OCA], [https://pdbe.org/4rnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rnd RCSB], [https://www.ebi.ac.uk/pdbsum/4rnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rnd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VATD_YEAST VATD_YEAST]] Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. [[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/VATD_YEAST VATD_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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<ref>PMID:23476018</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | ==See Also== |
| - | </div>
| + | *[[ATPase 3D structures|ATPase 3D structures]] |
| - | == References == | + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Balakrishna, A M]] | + | [[Category: Large Structures]] |
| - | [[Category: Basak, S]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gruber, G]] | + | [[Category: Balakrishna AM]] |
| - | [[Category: Alpha helical]] | + | [[Category: Basak S]] |
| - | [[Category: Coupling]] | + | [[Category: Gruber G]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Regulatory]]
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| - | [[Category: Rossmann fold]]
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