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| {{STRUCTURE_1kmh| PDB=1kmh | SCENE= }} | | {{STRUCTURE_1kmh| PDB=1kmh | SCENE= }} |
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| '''Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin'''
| | ===Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11904410}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11904410 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11904410}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Groth, G.]] | | [[Category: Groth, G.]] |
| [[Category: Protein-inhibitor complex]] | | [[Category: Protein-inhibitor complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:54:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:33:21 2008'' |
