1kmh
From Proteopedia
Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin
Structural highlights
Function[ATPA_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [ATPB_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTentoxin, 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. Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin.,Groth G Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3464-8. PMID:11904410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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