5gar: Difference between revisions

Revision as of 16:41, 26 July 2023

Thermus thermophilus V/A-ATPase, conformation 1Thermus thermophilus V/A-ATPase, conformation 1

5gar, resolution 6.40Å

Structural highlights

5gar is a 26 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 6.4Å
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VATA_THET8 Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.

Publication Abstract from PubMed

Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacteriumThermus thermophilusis similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined theT. thermophilusV/A-ATPase structure by cryo-EM at 6.4 A resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequence within the map, providing a complete model of the rotary ATPase. Comparing the membrane-embedded regions of theT. thermophilusV/A-ATPase and eukaryotic V-ATPase fromSaccharomyces cerevisiaeallowed identification of the alpha-helices that belong to the a subunit and revealed the existence of previously unknown subunits in the eukaryotic enzyme. Subsequent evolutionary covariance analysis enabled construction of a model of the a subunit in theS. cerevisaeV-ATPase that explains numerous biochemical studies of that enzyme. Comparing the two a subunit structures determined here with a structure of the distantly related a subunit from the bovine F-type ATP synthase revealed a conserved pattern of residues, suggesting a common mechanism for proton transport in all rotary ATPases.

Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.,Schep DG, Zhao J, Rubinstein JL Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3245-50. doi:, 10.1073/pnas.1521990113. Epub 2016 Mar 7. PMID:26951669^[1]

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

References

↑ Schep DG, Zhao J, Rubinstein JL. Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance. Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3245-50. doi:, 10.1073/pnas.1521990113. Epub 2016 Mar 7. PMID:26951669 doi:http://dx.doi.org/10.1073/pnas.1521990113

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OCA

[1] Schep DG, Zhao J, Rubinstein JL. Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance. Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3245-50. doi:, 10.1073/pnas.1521990113. Epub 2016 Mar 7. PMID:26951669 doi:http://dx.doi.org/10.1073/pnas.1521990113

[1]

@@ Line 3: / Line 3: @@
 <SX load='5gar' size='340' side='right' viewer='molstar' caption='[[5gar]], [[Resolution|resolution]] 6.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gar]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GAR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GAR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gar]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GAR FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gas|5gas]], [[5i1m|5i1m]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.4&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></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=5gar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gar OCA], [https://pdbe.org/5gar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gar RCSB], [https://www.ebi.ac.uk/pdbsum/5gar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gar ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gar OCA], [http://pdbe.org/5gar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gar RCSB], [http://www.ebi.ac.uk/pdbsum/5gar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gar ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VATF_THET8 VATF_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATE_THET8 VATE_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATB_THET2 VATB_THET2]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/VATA_THET8 VATA_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. [[http://www.uniprot.org/uniprot/VATD_THET2 VATD_THET2]] Produces ATP from ADP in the presence of a proton gradient across the membrane.
+[https://www.uniprot.org/uniprot/VATA_THET8 VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 28: / Line 27: @@
 [[Category: Large Structures]]
 [[Category: Thermus thermophilus]]
-[[Category: Rubinstein, J L]]
+[[Category: Rubinstein JL]]
-[[Category: Schep, D G]]
+[[Category: Schep DG]]
-[[Category: Zhao, J]]
+[[Category: Zhao J]]
-[[Category: A-atpase]]
-[[Category: Hydrolase]]
-[[Category: Membrane protein]]
-[[Category: Rotary atpase]]
-[[Category: V-atpase]]
-[[Category: V/a-atpase]]

5gar: Difference between revisions

Revision as of 16:41, 26 July 2023

Thermus thermophilus V/A-ATPase, conformation 1Thermus thermophilus V/A-ATPase, conformation 1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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5gar: Difference between revisions

Revision as of 16:41, 26 July 2023

Thermus thermophilus V/A-ATPase, conformation 1Thermus thermophilus V/A-ATPase, conformation 1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search