4efa

From Proteopedia

(Difference between revisions)

Revision as of 21:58, 24 December 2014

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

Structural highlights

4efa is a 3 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.
Ligands:
Related:	4dl0
Gene:	VAT3, VATC, VMA5, YKL080W, YKL410 (Saccharomyces cerevisiae S288c), VMA10, YHR039BC, YHR039C-A, YHR039C-B (Saccharomyces cerevisiae S288c), O6241, VAT5, VMA4, YOR332W (Saccharomyces cerevisiae S288c)
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VATC_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.^[1] [VATE_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [VATG_YEAST] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Publication Abstract from PubMed

Vacuolar ATPases (V-ATPases) are multisubunit rotary motor proton pumps that function to acidify subcellular organelles in all eukaryotic organisms. V-ATPase is regulated by a unique mechanism that involves reversible dissociation into V(1)-ATPase and V(o) proton channel, a process that involves breaking of protein interactions mediated by subunit C, the cytoplasmic domain of subunit "a" and three "peripheral stalks," each made of a heterodimer of E and G subunits. Here, we present crystal structures of a yeast V-ATPase heterotrimeric complex composed of EG heterodimer and the head domain of subunit C (C(head)). The structures show EG heterodimer folded in a noncanonical coiled coil that is stabilized at its N-terminal ends by binding to C(head). The coiled coil is disrupted by a bulge of partially unfolded secondary structure in subunit G and we speculate that this unique feature in the eukaryotic V-ATPase peripheral stalk may play an important role in enzyme structure and regulation by reversible dissociation.

Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGC(head) Peripheral Stalk Complex.,Oot RA, Huang LS, Berry EA, Wilkens S Structure. 2012 Sep 18. pii: S0969-2126(12)00321-8. doi:, 10.1016/j.str.2012.08.020. PMID:23000382^[2]

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

References

↑ Parra KJ, Keenan KL, Kane PM. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J Biol Chem. 2000 Jul 14;275(28):21761-7. PMID:10781598 doi:http://dx.doi.org/10.1074/jbc.M002305200
↑ Oot RA, Huang LS, Berry EA, Wilkens S. Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGC(head) Peripheral Stalk Complex. Structure. 2012 Sep 18. pii: S0969-2126(12)00321-8. doi:, 10.1016/j.str.2012.08.020. PMID:23000382 doi:http://dx.doi.org/10.1016/j.str.2012.08.020

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/4efa"

@@ Line 9: / Line 9: @@
 <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=4efa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4efa RCSB], [http://www.ebi.ac.uk/pdbsum/4efa PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VATC_YEAST VATC_YEAST]] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:10781598</ref>  [[http://www.uniprot.org/uniprot/VATE_YEAST VATE_YEAST]] Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. [[http://www.uniprot.org/uniprot/VATG_YEAST VATG_YEAST]] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4efa

From Proteopedia

Revision as of 21:58, 24 December 2014

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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