6hh0: Difference between revisions
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<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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6hh0]] is a 1 chain structure. 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 [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> | ||
</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> | </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> | ||
<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> | </table> | ||
== Function == | == 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> | [[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> | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30209131</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6hh0" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | |||
[[Category: Hohlweg, W]] | [[Category: Hohlweg, W]] | ||
[[Category: Wagner, G]] | [[Category: Wagner, G]] | ||
Revision as of 11:44, 26 September 2018
Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micellesYeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles
Structural highlights
Function[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.[1] [2] [3] Publication Abstract from PubMedVacuolar 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
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