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1kmh

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Revision as of 21:30, 24 January 2018

Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin

Structural highlights

1kmh is a 2 chain structure with sequence from Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fx0
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

↑ Groth G. Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3464-8. PMID:11904410 doi:10.1073/pnas.052546099

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kmh"

Categories: Spinacia oleracea | Groth, G | Hydrolase | Protein-inhibitor complex

@@ Line 1: / Line 1: @@
 ==Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin==
 <StructureSection load='1kmh' size='340' side='right' caption='[[1kmh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fx0|1fx0]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1kmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmh RCSB], [http://www.ebi.ac.uk/pdbsum/1kmh PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1kmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmh RCSB], [http://www.ebi.ac.uk/pdbsum/1kmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1kmh" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[ATPase|ATPase]]
 == References ==
 <references/>

1kmh

From Proteopedia

Revision as of 21:30, 24 January 2018

Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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