1kmh
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=TTX:TENTOXIN'>TTX</scene> | |LIGAND= <scene name='pdbligand=TTX:TENTOXIN'>TTX</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fx0|1FX0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmh OCA], [http://www.ebi.ac.uk/pdbsum/1kmh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kmh RCSB]</span> | ||
}} | }} | ||
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[[Category: Spinacia oleracea]] | [[Category: Spinacia oleracea]] | ||
[[Category: Groth, G.]] | [[Category: Groth, G.]] | ||
| - | [[Category: TTX]] | ||
[[Category: protein-inhibitor complex]] | [[Category: protein-inhibitor complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:35 2008'' |
Revision as of 18:50, 30 March 2008
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| , resolution 3.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Related: | 1FX0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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