1kmh
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1kmh.gif|left|200px]] | [[Image:1kmh.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1kmh", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1kmh| PDB=1kmh | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin''' | '''Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11904410 11904410] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11904410 11904410] | ||
| - | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Spinacia oleracea]] | [[Category: Spinacia oleracea]] | ||
[[Category: Groth, G.]] | [[Category: Groth, G.]] | ||
| - | [[Category: | + | [[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 | + | |
Revision as of 19:55, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 22:54:59 2008
