9bry: Difference between revisions

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-'''Unreleased structure'''
-The entry 9bry is ON HOLD
+==V0-only V-ATPase in synaptophysin gene knock-out mouse brain isolated synaptic vesicles==
+<StructureSection load='9bry' size='340' side='right'caption='[[9bry]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9bry]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BRY FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=9bry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bry OCA], [https://pdbe.org/9bry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bry RCSB], [https://www.ebi.ac.uk/pdbsum/9bry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bry ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VAS1_MOUSE VAS1_MOUSE] Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed:18713856). 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). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (PubMed:18713856).[UniProtKB:Q15904]<ref>PMID:18713856</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Brunger AT]]
+[[Category: Guo Q]]
+[[Category: Jiang W]]
+[[Category: Wang C]]
+[[Category: Wang X]]
+[[Category: Yang K]]