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6r0z

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Revision as of 23:57, 6 March 2020

Thermus thermophilus V/A-type ATPase/synthase, rotational state 1L

6r0z, resolution 3.80Å

Structural highlights

6r0z 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, 6r0w, 6r0y, 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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6r0z"

@@ Line 1: / Line 1: @@
 ==Thermus thermophilus V/A-type ATPase/synthase, rotational state 1L==
-<StructureSection load='6r0z' size='340' side='right'caption='[[6r0z]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<SX load='6r0z' size='340' side='right' viewer='molstar' caption='[[6r0z]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6r0z]] 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=6R0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R0Z FirstGlance]. <br>
@@ Line 23: / Line 23: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Large Structures]]
 [[Category: Thet8]]

6r0z

From Proteopedia

Revision as of 23:57, 6 March 2020

Thermus thermophilus V/A-type ATPase/synthase, rotational state 1L

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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