|
|
| Line 3: |
Line 3: |
| <StructureSection load='6vqh' size='340' side='right'caption='[[6vqh]], [[Resolution|resolution]] 4.40Å' scene=''> | | <StructureSection load='6vqh' size='340' side='right'caption='[[6vqh]], [[Resolution|resolution]] 4.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6vqh]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VQH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VQH FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6vqh]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VQH FirstGlance]. <br> |
| </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vqh OCA], [http://pdbe.org/6vqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vqh RCSB], [http://www.ebi.ac.uk/pdbsum/6vqh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vqh ProSAT]</span></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</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=6vqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vqh OCA], [https://pdbe.org/6vqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vqh RCSB], [https://www.ebi.ac.uk/pdbsum/6vqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vqh ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/Q5M7T6_RAT Q5M7T6_RAT]] Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar 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.[PIRNR:PIRNR018497] [[http://www.uniprot.org/uniprot/VPP1_RAT VPP1_RAT]] Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity). [[http://www.uniprot.org/uniprot/VA0E2_RAT VA0E2_RAT]] Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [[http://www.uniprot.org/uniprot/VATL_RAT VATL_RAT]] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). [[http://www.uniprot.org/uniprot/VATF_RAT VATF_RAT]] 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. [[http://www.uniprot.org/uniprot/RENR_RAT RENR_RAT]] Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the proton-transporting vacuolar (V)-ATPase protein pump. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS) (By similarity). Probably by controlling the assembly of the V-ATPase pump and thus the acidification of the endo-lysosomal system, plays a role in many neuronal processes including synapse morphology and synaptic transmission (By similarity).[UniProtKB:O75787][UniProtKB:Q9CYN9] [[http://www.uniprot.org/uniprot/VAS1_RAT VAS1_RAT]] Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity).[UniProtKB:Q15904] | | [https://www.uniprot.org/uniprot/Q5M7T6_RAT Q5M7T6_RAT] Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar 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.[PIRNR:PIRNR018497] |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a Legionella pneumophila effector protein. Cryo-electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in both Wnt signaling and the renin-angiotensin system that regulates blood pressure. This structure shows how ATP6AP1/Ac45 and ATP6AP2/PRR enable assembly of the enzyme's catalytic and membrane regions.
| |
| | |
| Structure of V-ATPase from the mammalian brain.,Abbas YM, Wu D, Bueler SA, Robinson CV, Rubinstein JL Science. 2020 Mar 13;367(6483):1240-1246. doi: 10.1126/science.aaz2924. PMID:32165585<ref>PMID:32165585</ref>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 6vqh" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[ATPase 3D structures|ATPase 3D structures]] | | *[[ATPase 3D structures|ATPase 3D structures]] |
| == References ==
| | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| [[Category: Abbas, Y M]] | | [[Category: Abbas YM]] |
| [[Category: Rubinstein, J L]] | | [[Category: Rubinstein JL]] |
| [[Category: Membrane protein complex]]
| |
| [[Category: Proton transport]]
| |
| [[Category: Rotary atpase]]
| |