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| | <StructureSection load='1xg2' size='340' side='right'caption='[[1xg2]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1xg2' size='340' side='right'caption='[[1xg2]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xg2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actch Actch] and [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XG2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xg2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis] and [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XG2 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xg2 OCA], [https://pdbe.org/1xg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1xg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xg2 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xg2 OCA], [https://pdbe.org/1xg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1xg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xg2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PME1_SOLLC PME1_SOLLC]] Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening. [[https://www.uniprot.org/uniprot/PMEI_ACTDE PMEI_ACTDE]] Inhibits pectin methylesterase; may be involved in the regulation of fruit ripening.
| + | [https://www.uniprot.org/uniprot/PME1_SOLLC PME1_SOLLC] Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actch]] | + | [[Category: Actinidia chinensis]] |
| - | [[Category: Hydrolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Solanum lycopersicum]] | | [[Category: Solanum lycopersicum]] |
| - | [[Category: Bellincampi, D]] | + | [[Category: Bellincampi D]] |
| - | [[Category: Bonivento, D]] | + | [[Category: Bonivento D]] |
| - | [[Category: Camardella, L]] | + | [[Category: Camardella L]] |
| - | [[Category: Cervone, F]] | + | [[Category: Cervone F]] |
| - | [[Category: Giovane, A]] | + | [[Category: De Lorenzo G]] |
| - | [[Category: Lorenzo, G De]] | + | [[Category: Di Matteo A]] |
| - | [[Category: Matteo, A Di]] | + | [[Category: Giovane A]] |
| - | [[Category: Raiola, A]] | + | [[Category: Raiola A]] |
| - | [[Category: Tsernoglou, D]] | + | [[Category: Tsernoglou D]] |
| - | [[Category: Beta helix]]
| + | |
| - | [[Category: Four helix bundle]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| Structural highlights
Function
PME1_SOLLC Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening.
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
Pectin, one of the main components of the plant cell wall, is secreted in a highly methyl-esterified form and subsequently deesterified in muro by pectin methylesterases (PMEs). In many developmental processes, PMEs are regulated by either differential expression or posttranslational control by protein inhibitors (PMEIs). PMEIs are typically active against plant PMEs and ineffective against microbial enzymes. Here, we describe the three-dimensional structure of the complex between the most abundant PME isoform from tomato fruit (Lycopersicon esculentum) and PMEI from kiwi (Actinidia deliciosa) at 1.9-A resolution. The enzyme folds into a right-handed parallel beta-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long alpha-helices aligned in an antiparallel manner in a classical up-and-down four-helical bundle. The two proteins form a stoichiometric 1:1 complex in which the inhibitor covers the shallow cleft of the enzyme where the putative active site is located. The four-helix bundle of the inhibitor packs roughly perpendicular to the main axis of the parallel beta-helix of PME, and three helices of the bundle interact with the enzyme. The interaction interface displays a polar character, typical of nonobligate complexes formed by soluble proteins. The structure of the complex gives an insight into the specificity of the inhibitor toward plant PMEs and the mechanism of regulation of these enzymes.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.,Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D Plant Cell. 2005 Mar;17(3):849-58. Epub 2005 Feb 18. PMID:15722470[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D. Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein. Plant Cell. 2005 Mar;17(3):849-58. Epub 2005 Feb 18. PMID:15722470 doi:10.1105/tpc.104.028886
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