2lx4

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==NMR solution structure of peptide a2N(1-17) from Mus musculus V-ATPase==
==NMR solution structure of peptide a2N(1-17) from Mus musculus V-ATPase==
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<StructureSection load='2lx4' size='340' side='right'caption='[[2lx4]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2lx4' size='340' side='right'caption='[[2lx4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lx4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LX4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lx4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LX4 FirstGlance]. <br>
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</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=2lx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lx4 OCA], [https://pdbe.org/2lx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lx4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lx4 ProSAT]</span></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">Solution NMR</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=2lx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lx4 OCA], [https://pdbe.org/2lx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lx4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lx4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/VPP2_MOUSE VPP2_MOUSE]] Part of the proton channel of V-ATPases (By similarity). Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH.<ref>PMID:16415858</ref>
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[https://www.uniprot.org/uniprot/VPP2_MOUSE VPP2_MOUSE] Part of the proton channel of V-ATPases (By similarity). Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH.<ref>PMID:16415858</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Previously, we reported an acidification-dependent interaction of the endosomal V-ATPase with cytohesin-2, a GDP/GTP-exchange factor (GEF), suggesting that it functions as a pH-sensing receptor. Here, we have studied the molecular mechanism of signaling between the V-ATPase, cytohesin-2 and Arf GTP-binding proteins. We found that part of the N-terminal cytosolic tail of the V-ATPase a2-subunit (a2N), corresponding to its first seventeen amino acids (a2N(1-17)), potently modulates the enzymatic GDP/GTP-exchange activity of cytohesin-2. Moreover, this peptide strongly inhibits GEF-activity via direct interaction with the Sec7 domain of cytohesin-2. The structure of a2N(1-17) and its amino acids F(5), M(10) and Q(14) involved in interaction with Sec7 domain were determined by NMR spectroscopy analysis. In silico docking experiments revealed that part of the V-ATPase formed by its a2N(1-17) epitope competes with the Switch 2 region of Arf1 and Arf6 for binding to the Sec7 domain of cytohesin-2. The amino acid sequence alignment and GEF-activity studies also uncovered the conserved character of signaling between all four (a1-a4) a-subunit isoforms of mammalian V-ATPase and cytohesin-2. Moreover, the conserved character of this phenomenon was also confirmed in experiments showing binding of mammalian cytohesin-2 to the intact yeast V-ATPase holo-complex. Thus, here we have uncovered an evolutionarily conserved function of the V-ATPase as a novel cytohesin-signaling receptor.
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The N-terminus of a-Subunit Isoforms is Involved in Signaling between V-ATPase and Cytohesin-2.,Hosokawa H, Dip PV, Merkulova M, Bakulina A, Zhuang Z, Khatri A, Jian X, Keating SM, Bueler SA, Rubinstein JL, Randazzo PA, Ausiello DA, Gruber G, Marshansky V J Biol Chem. 2013 Jan 3. PMID:23288846<ref>PMID:23288846</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 2lx4" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dip, P]]
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[[Category: Mus musculus]]
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[[Category: Gruber, G]]
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[[Category: Dip P]]
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[[Category: Marshansky, V]]
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[[Category: Gruber G]]
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[[Category: Alpha helix]]
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[[Category: Marshansky V]]
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[[Category: Ph sensor]]
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[[Category: Proton transport]]
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[[Category: Sec7 binding motif]]
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[[Category: Subunit some]]
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[[Category: V-atpase]]
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Current revision

NMR solution structure of peptide a2N(1-17) from Mus musculus V-ATPase

PDB ID 2lx4

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