1KMH

Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin

Summary for 1KMH

• Entry DOI: 10.2210/pdb1kmh/pdb
• Related: 1FX0
• Descriptor: ATPase alpha subunit, ATPase beta subunit, TENTOXIN (3 entities in total)
• Functional Keywords: protein-inhibitor complex, hydrolase
• Biological source: Spinacia oleracea (spinach); More
• Total number of polymer chains: 2
• Total formula weight: 109841.27

Authors

Groth, G. (deposition date: 2001-12-16, release date: 2002-03-13, Last modification date: 2024-12-25)

Primary citation

Groth, G.
Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin.
Proc.Natl.Acad.Sci.USA, 99:3464-3468, 2002

PubMed Abstract: Tentoxin, a natural cyclic tetrapeptide produced by phytopathogenic fungi from the Alternaria species affects the catalytic function of the chloroplast F(1)-ATPase in certain sensitive species of plants. In this study, we show that the uncompetitive inhibitor tentoxin binds to the alphabeta-interface of the chloroplast F(1)-ATPase in a cleft localized at betaAsp-83. Most of the binding site is located on the noncatalytic alpha-subunit. The crystal structure of the tentoxin-inhibited CF(1)-complex suggests that the inhibitor is hydrogen bonded to Asp-83 in the catalytic beta-subunit but forms hydrophobic contacts with residues Ile-63, Leu-65, Val-75, Tyr-237, Leu-238, and Met-274 in the adjacent alpha-subunit. Except for minor changes around the tentoxin-binding site, the structure of the chloroplast alpha(3)beta(3)-core complex is the same as that determined with the native chloroplast ATPase. Tentoxin seems to act by inhibiting inter-subunit contacts at the alphabeta-interface and by blocking the interconversion of binding sites in the catalytic mechanism.

PubMed: 11904410
DOI: 10.1073/pnas.052546099

Experimental method

X-RAY DIFFRACTION (3.4 Å)