5gas

From Proteopedia

(Difference between revisions)

Revision as of 20:04, 10 April 2020

Thermus thermophilus V/A-ATPase, conformation 2

5gas, resolution 9.50Å

Structural highlights

5gas 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.
Related:	5gar, 5i1m
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATE_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATC_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [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. [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. [VATD_THET2] Produces ATP from ADP in the presence of a proton gradient across the membrane.

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

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/5gas"

@@ Line 3: / Line 3: @@
 <SX load='5gas' size='340' side='right' viewer='molstar' caption='[[5gas]], [[Resolution|resolution]] 9.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gas]] 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=5GAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GAS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gas]] 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=5GAS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GAS FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gar|5gar]], [[5i1m|5i1m]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gas OCA], [http://pdbe.org/5gas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gas RCSB], [http://www.ebi.ac.uk/pdbsum/5gas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gas 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=5gas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gas OCA], [http://pdbe.org/5gas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gas RCSB], [http://www.ebi.ac.uk/pdbsum/5gas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gas ProSAT]</span></td></tr>
 </table>
 == Function ==

5gas

From Proteopedia

Revision as of 20:04, 10 April 2020

Thermus thermophilus V/A-ATPase, conformation 2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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