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5y5x

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Revision as of 20:12, 6 March 2020

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

5y5x, resolution 5.00Å

Structural highlights

5y5x is a 26 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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

[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

Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H(+)-rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V1 domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane.

Cryo EM structure of intact rotary H(+)-ATPase/synthase from Thermus thermophilus.,Nakanishi A, Kishikawa JI, Tamakoshi M, Mitsuoka K, Yokoyama K Nat Commun. 2018 Jan 8;9(1):89. doi: 10.1038/s41467-017-02553-6. PMID:29311594^[1]

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

References

↑ Nakanishi A, Kishikawa JI, Tamakoshi M, Mitsuoka K, Yokoyama K. Cryo EM structure of intact rotary H(+)-ATPase/synthase from Thermus thermophilus. Nat Commun. 2018 Jan 8;9(1):89. doi: 10.1038/s41467-017-02553-6. PMID:29311594 doi:http://dx.doi.org/10.1038/s41467-017-02553-6

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/5y5x"

@@ Line 1: / Line 1: @@
 ==V/A-type ATPase/synthase from Thermus thermophilus, rotational state 1==
-<StructureSection load='5y5x' size='340' side='right'caption='[[5y5x]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
+<SX load='5y5x' size='340' side='right' viewer='molstar' caption='[[5y5x]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5y5x]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y5X FirstGlance]. <br>
@@ Line 25: / Line 25: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Large Structures]]
 [[Category: Thermus thermophilus hb8]]

5y5x

From Proteopedia

Revision as of 20:12, 6 March 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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