PDBsum entry 2qe7

Hydrolase

PDB id: 2qe7

Contents

Protein chains

474 a.a. *

461 a.a. *

227 a.a. *

135 a.a. *

* Residue conservation analysis

PDB id:

2qe7

Name:

Hydrolase

Title:

Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. Ta2.A1

Structure:

Atp synthase subunit alpha. Chain: a, b, c. Engineered: yes. Atp synthase subunit beta. Chain: d, e, f. Engineered: yes. Atp synthase subunit gamma. Chain: g. Engineered: yes.

Source:

Bacillus sp.. Organism_taxid: 90973. Strain: ta2.A1. Gene: atpa. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: atpd. Gene: atpg. Gene: atpc.

Resolution:

3.06Å R-factor: 0.252 R-free: 0.306

Authors:

A.Stocker,S.Keis,J.Vonck,G.M.Cook,P.Dimroth

Key ref:

A.Stocker et al. (2007). The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase. Structure, 15, 904-914. PubMed id: 17697996 DOI: 10.1016/j.str.2007.06.009

Date:

25-Jun-07 Release date: 21-Aug-07

Protein chains

Q71CG5  (Q71CG5_9BACI) -  ATP synthase subunit alpha from Bacillus sp. TA2.A1

Seq: 502 a.a.

Struc: 474 a.a.

Protein chains

Q71CG3  (Q71CG3_9BACI) -  ATP synthase subunit beta from Bacillus sp. TA2.A1

Seq: 462 a.a.

Struc: 461 a.a.

Protein chain

Q71CG4  (Q71CG4_9BACI) -  ATP synthase gamma chain from Bacillus sp. TA2.A1

Seq: 286 a.a.

Struc: 227 a.a.

Protein chain

Q71CG2  (Q71CG2_9BACI) -  ATP synthase epsilon chain from Bacillus sp. TA2.A1

Seq: 135 a.a.

Struc: 135 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B, C, D, E, F: E.C.7.1.2.2 - H(+)-transporting two-sector ATPase.
• Reaction: ATP + H2O + 4 H⁺(in) = ADP + phosphate + 5 H⁺(out)
• Enzyme class 3: Chains G, H: E.C.3.6.1.34 - Transferred entry: 7.1.2.2.

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2007.06.009

Structure 15:904-914 (2007)

PubMed id: 17697996

The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase.

A.Stocker, S.Keis, J.Vonck, G.M.Cook, P.Dimroth.

ABSTRACT

The ATP synthase of the thermoalkaliphilic Bacillus sp. TA2.A1 operates exclusively in ATP synthesis direction. In the crystal structure of the nucleotide-free alpha(3)beta(3)gamma epsilon subcomplex (TA2F(1)) at 3.1 A resolution, all three beta subunits adopt the open beta(E) conformation. The structure shows salt bridges between the helix-turn-helix motif of the C-terminal domain of the beta(E) subunit (residues Asp372 and Asp375) and the N-terminal helix of the gamma subunit (residues Arg9 and Arg10). These electrostatic forces pull the gamma shaft out of the rotational center and impede rotation through steric interference with the beta(E) subunit. Replacement of Arg9 and Arg10 with glutamines eliminates the salt bridges and results in an activation of ATP hydrolysis activity, suggesting that these salt bridges prevent the native enzyme from rotating in ATP hydrolysis direction. A similar bending of the gamma shaft as in the TA2F(1) structure was observed by single-particle analysis of the TA2F(1)F(o) holoenzyme.

Selected figure(s)

Figure 1.
Figure 1. Stereo Drawings of the Three-Dimensional Structure of the α[3]β[3]γ epsilon Subcomplex of F[1] from the Thermoalkaliphilic Bacillus sp. TA2.A1
(A) Side view of the complex with the pseudo three-fold axis vertical. Three structural domains are visible in each subunit of the α[3]β[3] hexamer. The β and α subunits are shown in pink and pale yellow, respectively. The γ subunit and the epsilon subunit with the highest occupancy are shown in light blue and lime, respectively.
(B) Top view of the complex viewed toward the membrane; the pseudo three-fold axis points toward the viewer.
(C) Bottom view of the complex viewed from the membrane.

Figure 5.
Figure 5. Electron Microscopic Analysis of Native TA2F[1]F[o]
(A) Electron micrograph of TA2F[1]F[o] negatively stained with uranyl acetate. The scale bar represents 50 nm.
(B) Class averages after multivariate statistical analysis and classification of 1940 particles. At least 20% of particles were rejected based on poor resolution, as well as 20% from each class. Classes 1–8 contain 197, 250, 197, 194, 184, 261, 141, and 129 particles, respectively. Classes 1–4 show a view with the central stalk attached asymmetrically on the left side of the c ring; classes 5–7 show a more centrally connected stalk and a much narrower F[o] domain. Class 8 contains some poorly aligned particles, of which some have the F[1] domain facing down. Each frame represents 382 Å.
(C) Corresponding views of the TA2F[1] structure rotated approximately 90° relative to each other. The images were created using UCSF Chimera (Pettersen et al., 2004).

The above figures are reprinted by permission from Cell Press: Structure (2007, 15, 904-914) copyright 2007.

Figures were selected by an automated process.