PDBsum entry 3k5b

Hydrolase

PDB id

3k5b

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Contents

			Protein chains

					100 a.a. *


					184 a.a. *

* Residue conservation analysis

PDB id:

3k5b

Links

Name:

Hydrolase

Title:

Crystal structure of the peripheral stalk of thermus thermophilus h+- atpase/synthase

Structure:

V-type atp synthase, subunit (vapc-therm). Chain: g, b. Fragment: g-17: n-terminally truncated by 17 residues. Engineered: yes. V-type atp synthase subunit e. Chain: e, a. Synonym: v-atpase subunit e. Engineered: yes. Mutation: yes

Source:

Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Gene: 55981248, ttha1279. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: 55981245, atpe, ttha1276, vate.

Resolution:

3.10Å

R-factor:

0.235

R-free:

0.288

Authors:

L.K.Lee,A.G.Stewart,M.Donohoe,R.A.Bernal,D.Stock

Key ref:

L.K.Lee et al. (2010). The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat Struct Biol, 17, 373-378. PubMed id: 20173764

Date:

07-Oct-09

Release date:

23-Feb-10

PROCHECK

	Headers

	References

Protein chains

Q5SIT5 (Q5SIT5_THET8) - V-type ATP synthase, subunit (VAPC-THERM) from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: Struc:					120 a.a. 100 a.a.

Protein chains

P74901 (VATE_THET8) - V-type ATP synthase subunit E from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: Struc:					188 a.a. 184 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

	Nat Struct Biol 17:373-378 (2010)
PubMed id: 20173764

The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase.
L.K.Lee, A.G.Stewart, M.Donohoe, R.A.Bernal, D.Stock.

ABSTRACT

Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 A resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases.

Literature references that cite this PDB file's key reference

PubMed id

Reference

23142977

S.Benlekbir, S.A.Bueler, and J.L.Rubinstein (2012).
Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution.

Nat Struct Mol Biol, 19, 1356-1362.

21368147

A.Wächter, Y.Bi, S.D.Dunn, B.D.Cain, H.Sielaff, F.Wintermann, S.Engelbrecht, and W.Junge (2011).
Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.

Proc Natl Acad Sci U S A, 108, 3924-3929.

21269440

Y.Peng, Y.Luo, T.Yu, X.Xu, K.Fan, Y.Zhao, and K.Yang (2011).
A Blue Native-PAGE analysis of membrane protein complexes in Clostridium thermocellum.

BMC Microbiol, 11, 22.

20571891

A.M.Balakrishna, M.S.Manimekalai, C.Hunke, S.Gayen, M.Rössle, J.Jeyakanthan, and G.Grüber (2010).
Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering.

J Bioenerg Biomembr, 42, 311-320.

PDB code:

3lg8

20838636

Z.L.Hildenbrand, S.K.Molugu, D.Stock, and R.A.Bernal (2010).
The C-H peripheral stalk base: a novel component in V1-ATPase assembly.

PLoS One, 5, e12588.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.