5d80

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form

Structural highlights

5d80 is a 30 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 6.202Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VATA_YEAST Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.^[1] PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.^[2]

Publication Abstract from PubMed

Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V-ATPase activity is regulated by a unique mechanism referred to as reversible disassembly, wherein the soluble catalytic sector, V1, is released from the membrane and its MgATPase activity silenced. The crystal structure of yeast V1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C-terminal domain rotating ~150 degrees from a position near the membrane in holo V-ATPase to a position at the bottom of V1 near an open catalytic site. Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site.

Crystal structure of yeast V1-ATPase in the autoinhibited state.,Oot RA, Kane PM, Berry EA, Wilkens S EMBO J. 2016 Jun 13. pii: e201593447. PMID:27295975^[3]

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

References

↑ Gimble FS, Thorner J. Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae. Nature. 1992 May 28;357(6376):301-6. PMID:1534148 doi:http://dx.doi.org/10.1038/357301a0
↑ Gimble FS, Thorner J. Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae. Nature. 1992 May 28;357(6376):301-6. PMID:1534148 doi:http://dx.doi.org/10.1038/357301a0
↑ Oot RA, Kane PM, Berry EA, Wilkens S. Crystal structure of yeast V1-ATPase in the autoinhibited state. EMBO J. 2016 Jun 13. pii: e201593447. PMID:27295975 doi:http://dx.doi.org/10.15252/embj.201593447

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/5d80"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5d80 is ON HOLD
+==Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form==
+<StructureSection load='5d80' size='340' side='right'caption='[[5d80]], [[Resolution|resolution]] 6.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5d80]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D80 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.202&#8491;</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=5d80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d80 OCA], [https://pdbe.org/5d80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d80 RCSB], [https://www.ebi.ac.uk/pdbsum/5d80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d80 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VATA_YEAST VATA_YEAST] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.<ref>PMID:1534148</ref>   PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.<ref>PMID:1534148</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V-ATPase activity is regulated by a unique mechanism referred to as reversible disassembly, wherein the soluble catalytic sector, V1, is released from the membrane and its MgATPase activity silenced. The crystal structure of yeast V1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C-terminal domain rotating ~150 degrees from a position near the membrane in holo V-ATPase to a position at the bottom of V1 near an open catalytic site. Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site.
-Authors: Oot, R.A., Kane, P.M., Berry, E.A., Wilkens, S.
+Crystal structure of yeast V1-ATPase in the autoinhibited state.,Oot RA, Kane PM, Berry EA, Wilkens S EMBO J. 2016 Jun 13. pii: e201593447. PMID:27295975<ref>PMID:27295975</ref>
-Description: Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Kane, P.M]]
+<div class="pdbe-citations 5d80" style="background-color:#fffaf0;"></div>
-[[Category: Wilkens, S]]
-[[Category: Oot, R.A]]
+==See Also==
-[[Category: Berry, E.A]]
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Berry EA]]
+[[Category: Kane PM]]
+[[Category: Oot RA]]
+[[Category: Wilkens S]]

5d80

From Proteopedia

Current revision

Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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