6vq8

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Current revision (14:39, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6vq8' size='340' side='right'caption='[[6vq8]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<StructureSection load='6vq8' size='340' side='right'caption='[[6vq8]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6vq8]] is a 34 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VQ8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vq8]] is a 22 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=6VQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VQ8 FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg0968 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vq8 OCA], [http://pdbe.org/6vq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vq8 RCSB], [http://www.ebi.ac.uk/pdbsum/6vq8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vq8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vq8 OCA], [https://pdbe.org/6vq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vq8 RCSB], [https://www.ebi.ac.uk/pdbsum/6vq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vq8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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] [[http://www.uniprot.org/uniprot/Q8R2H0_RAT Q8R2H0_RAT]] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.[RuleBase:RU364019] [[http://www.uniprot.org/uniprot/VATB2_RAT VATB2_RAT]] Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. 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/VA0E2_RAT VA0E2_RAT]] Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [[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/VATC1_RAT VATC1_RAT]] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). [[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/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/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/VATE1_RAT VATE1_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.
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[https://www.uniprot.org/uniprot/D4A133_RAT D4A133_RAT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vq8" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Legph]]
 
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Abbas, Y M]]
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[[Category: Abbas YM]]
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[[Category: Rubinstein, J L]]
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[[Category: Rubinstein JL]]
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[[Category: Membrane protein complex]]
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[[Category: Proton transport]]
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[[Category: Rotary atpase]]
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Current revision

Mammalian V-ATPase from rat brain - composite model of rotational state 3 bound to ADP and SidK (built from focused refinement models)

PDB ID 6vq8

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