1FX0

Crystal structure of the chloroplast F1-ATPase from spinach

Summary for 1FX0

• Entry DOI: 10.2210/pdb1fx0/pdb
• Descriptor: ATP SYNTHASE ALPHA CHAIN, ATP SYNTHASE BETA CHAIN (2 entities in total)
• Functional Keywords: latent atpase, thermal stability, potential tentoxin binding site, hydrolase
• Biological source: Spinacia oleracea (spinach); More
• Cellular location: Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein : P06450 P00825
• Total number of polymer chains: 2
• Total formula weight: 109426.77

Authors

Groth, G.,Pohl, E. (deposition date: 2000-09-25, release date: 2001-09-25, Last modification date: 2024-02-07)

Primary citation

Groth, G.,Pohl, E.
The structure of the chloroplast F1-ATPase at 3.2 A resolution.
J.Biol.Chem., 276:1345-1352, 2001

PubMed Abstract: The structure of the F(1)-ATPase from spinach chloroplasts was determined to 3.2 A resolution by molecular replacement based on the homologous structure of the bovine mitochondrial enzyme. The crystallized complex contains four different subunits in a stoichiometry of alpha(3)beta(3)gammaepsilon. Subunit delta was removed before crystallization to improve the diffraction of the crystals. The overall structure of the noncatalytic alpha-subunits and the catalytic beta-subunits is highly similar to those of the mitochondrial and thermophilic subunits. However, in the crystal structure of the chloroplast enzyme, all alpha- and beta-subunits adopt a closed conformation and appear to contain no bound adenine nucleotides. The superimposed crystallographic symmetry in the space group R32 impaired an exact tracing of the gamma- and epsilon-subunits in the complex. However, clear electron density was present at the core of the alpha(3)beta(3)-subcomplex, which probably represents the C-terminal domain of the gamma-subunit. The structure of the spinach chloroplast F(1) has a potential binding site for the phytotoxin, tentoxin, at the alphabeta-interface near betaAsp(83) and an insertion from betaGly(56)-Asn(60) in the N-terminal beta-barrel domain probably increases the thermal stability of the complex. The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes.

PubMed: 11032839
DOI: 10.1074/jbc.M008015200

Experimental method

X-RAY DIFFRACTION (3.2 Å)