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4rnd

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Revision as of 17:25, 18 January 2017

Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.

Structural highlights

4rnd is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4ix9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VATD_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. [VATF_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.

Publication Abstract from PubMed

Eukaryotic V1VO-ATPases hydrolyze ATP in the V1 domain coupled to ion pumping in VO. A unique mode of regulation of V-ATPases is the reversible disassembly of V1 and VO, which reduces ATPase activity and causes silencing of ion conduction. The subunits D and F are proposed to be key in these enzymatic processes. Here, we describe the structures of two conformations of the subunit DF assembly of Saccharomyces cerevisiae (ScDF) V-ATPase at 3.1 A resolution. Subunit D (ScD) consists of a long pair of alpha-helices connected by a short helix ((79)IGYQVQE(85)) as well as a beta-hairpin region, which is flanked by two flexible loops. The long pair of helices is composed of the N-terminal alpha-helix and the C-terminal helix, showing structural alterations in the two ScDF structures. The entire subunit F (ScF) consists of an N-terminal domain of four beta-strands (beta1-beta4) connected by four alpha-helices (alpha1-alpha4). alpha1 and beta2 are connected via the loop (26)GQITPETQEK(35), which is unique in eukaryotic V-ATPases. Adjacent to the N-terminal domain is a flexible loop, followed by a C-terminal alpha-helix (alpha5). A perpendicular and extended conformation of helix alpha5 was observed in the two crystal structures and in solution x-ray scattering experiments, respectively. Fitted into the nucleotide-bound A3B3 structure of the related A-ATP synthase from Enterococcus hirae, the arrangements of the ScDF molecules reflect their central function in ATPase-coupled ion conduction. Furthermore, the flexibility of the terminal helices of both subunits as well as the loop (26)GQITPETQEK(35) provides information about the regulatory step of reversible V1VO disassembly.

Crystal Structure of Subunits D and F in Complex Gives Insight into Energy Transmission of the Eukaryotic V-ATPase from Saccharomyces cerevisiae.,Balakrishna AM, Basak S, Manimekalai MS, Gruber G J Biol Chem. 2015 Feb 6;290(6):3183-96. doi: 10.1074/jbc.M114.622688. Epub 2014, Dec 12. PMID:25505269^[1]

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

References

↑ Balakrishna AM, Basak S, Manimekalai MS, Gruber G. Crystal Structure of Subunits D and F in Complex Gives Insight into Energy Transmission of the Eukaryotic V-ATPase from Saccharomyces cerevisiae. J Biol Chem. 2015 Feb 6;290(6):3183-96. doi: 10.1074/jbc.M114.622688. Epub 2014, Dec 12. PMID:25505269 doi:http://dx.doi.org/10.1074/jbc.M114.622688

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/4rnd"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.==
 <StructureSection load='4rnd' size='340' side='right' caption='[[4rnd]], [[Resolution|resolution]] 3.18&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ix9|4ix9]]</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=4rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rnd RCSB], [http://www.ebi.ac.uk/pdbsum/4rnd PDBsum]</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=4rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnd OCA], [http://pdbe.org/4rnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rnd RCSB], [http://www.ebi.ac.uk/pdbsum/4rnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rnd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4rnd" style="background-color:#fffaf0;"></div>
 ==See Also==

4rnd

From Proteopedia

Revision as of 17:25, 18 January 2017

Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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