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6hh0

From Proteopedia

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Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles

Structural highlights

6hh0 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VPP1_YEAST Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1491220, PubMed:11278748). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:8798414, PubMed:11278748).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Vacuolar ATPases are multisubunit protein complexes that are indispensable for acidification and pH homeostasis in a variety of physiological processes in all eukaryotic cells. An arginine residue (Arg-735) in transmembrane helix 7 (TM7) of subunit a of the yeast ATPase is known to be essential for proton translocation. However, the specific mechanism of its involvement in proton transport remains to be determined. Arginine residues are usually assumed to "snorkel" toward the protein surface when exposed to a hydrophobic environment. Here, using solution NMR spectroscopy, molecular dynamics simulations and in vivo yeast assays, we obtained evidence for the formation of a transient, membrane-embedded cation-pi interaction in TM7 between Arg-735 and two highly conserved nearby aromatic residues, Tyr-733 and Trp-737. We propose a mechanism by which the transient, membrane-embedded cation-pi complex provides the necessary energy to keep the charged side chain of Arg-735 within the hydrophobic membrane. Such cation-pi interactions may define a general mechanism to retain charged amino acids in a hydrophobic membrane environment.

A cation-pi interaction in a transmembrane helix of vacuolar ATPase retains the proton transporting arginine in a hydrophobic environment.,Hohlweg W, Wagner GE, Hofbauer HF, Sarkleti F, Setz M, Gubensak N, Lichtenegger S, Falsone SF, Wolinski H, Kosol S, Oostenbrink C, Kohlwein SD, Zangger K J Biol Chem. 2018 Sep 12. pii: RA118.005276. doi: 10.1074/jbc.RA118.005276. PMID:30209131^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kawasaki-Nishi S, Nishi T, Forgac M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J Biol Chem. 2001 May 25;276(21):17941-8. Epub 2001 Mar 2. PMID:11278748 doi:http://dx.doi.org/10.1074/jbc.M010790200
↑ Manolson MF, Proteau D, Jones EW. Evidence for a conserved 95-120 kDa subunit associated with and essential for activity of V-ATPases. J Exp Biol. 1992 Nov;172:105-12. PMID:1491220
↑ Leng XH, Manolson MF, Liu Q, Forgac M. Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase. J Biol Chem. 1996 Sep 13;271(37):22487-93. PMID:8798414
↑ Hohlweg W, Wagner GE, Hofbauer HF, Sarkleti F, Setz M, Gubensak N, Lichtenegger S, Falsone SF, Wolinski H, Kosol S, Oostenbrink C, Kohlwein SD, Zangger K. A cation-pi interaction in a transmembrane helix of vacuolar ATPase retains the proton transporting arginine in a hydrophobic environment. J Biol Chem. 2018 Sep 12. pii: RA118.005276. doi: 10.1074/jbc.RA118.005276. PMID:30209131 doi:http://dx.doi.org/10.1074/jbc.RA118.005276

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6hh0"

Categories: Large Structures | Saccharomyces cerevisiae | Hohlweg W | Wagner G | Zangger K

@@ Line 1: / Line 1: @@
 ==Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles==
-<StructureSection load='6hh0' size='340' side='right' caption='[[6hh0]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='6hh0' size='340' side='right'caption='[[6hh0]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6hh0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HH0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6hh0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HH0 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPH1, YOR270C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</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=6hh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hh0 OCA], [https://pdbe.org/6hh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hh0 RCSB], [https://www.ebi.ac.uk/pdbsum/6hh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hh0 ProSAT]</span></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=6hh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hh0 OCA], [http://pdbe.org/6hh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hh0 RCSB], [http://www.ebi.ac.uk/pdbsum/6hh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hh0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VPH1_YEAST VPH1_YEAST]] Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref>
+[https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_YEAST] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:1491220, PubMed:8798414, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1491220, PubMed:11278748). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:8798414, PubMed:11278748).<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 17: @@
 </div>
 <div class="pdbe-citations 6hh0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Hohlweg, W]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Wagner, G]]
+[[Category: Hohlweg W]]
-[[Category: Zangger, K]]
+[[Category: Wagner G]]
-[[Category: Atpasse]]
+[[Category: Zangger K]]
-[[Category: Dpc micelle]]
-[[Category: Membrane protein]]
-[[Category: Nmr spectroscopy]]
-[[Category: Transmembrane helix]]

6hh0

From Proteopedia

Current revision

Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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