1kmh
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(New page: 200px<br /><applet load="1kmh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmh, resolution 3.40Å" /> '''Crystal Structure of...)
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Revision as of 17:14, 20 November 2007
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Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin
Overview
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.
About this Structure
1KMH is a Protein complex structure of sequences from Spinacia oleracea with TTX as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
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
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