6r0w

From Proteopedia

(Difference between revisions)

Current revision

Thermus thermophilus V/A-type ATPase/synthase, rotational state 2

6r0w, resolution 3.60Å

Structural highlights

6r0w is a 26 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	6qum, 6r0y, 6r0z, 6r10
Activity:	H(+)-transporting two-sector ATPase, with EC number 7.1.2.2
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VATE_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATD_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_THET8] 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. [VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane.

Publication Abstract from PubMed

V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family.

Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.,Zhou L, Sazanov LA Science. 2019 Aug 23;365(6455). pii: 365/6455/eaaw9144. doi:, 10.1126/science.aaw9144. PMID:31439765^[1]

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

References

↑ Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. 2019 Aug 23;365(6455). pii: 365/6455/eaaw9144. doi:, 10.1126/science.aaw9144. PMID:31439765 doi:http://dx.doi.org/10.1126/science.aaw9144

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/6r0w"

@@ Line 3: / Line 3: @@
 <SX load='6r0w' size='340' side='right' viewer='molstar' caption='[[6r0w]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6r0w]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R0W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6r0w]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6R0W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qum|6qum]], [[6r0y|6r0y]], [[6r0z|6r0z]], [[6r10|6r10]]</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=7.1.2.2 7.1.2.2] </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=6r0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0w OCA], [http://pdbe.org/6r0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0w RCSB], [http://www.ebi.ac.uk/pdbsum/6r0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0w 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=6r0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0w OCA], [http://pdbe.org/6r0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0w RCSB], [http://www.ebi.ac.uk/pdbsum/6r0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0w ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 6r0w" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>

6r0w

From Proteopedia

Current revision

Thermus thermophilus V/A-type ATPase/synthase, rotational state 2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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