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| | <StructureSection load='1x90' size='340' side='right'caption='[[1x90]], [[Resolution|resolution]] 2.68Å' scene=''> | | <StructureSection load='1x90' size='340' side='right'caption='[[1x90]], [[Resolution|resolution]] 2.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x90]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X90 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X90 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x90]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X90 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x8z|1x8z]], [[1x91|1x91]]</div></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]] 2.68Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT1G48020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=1x90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x90 OCA], [https://pdbe.org/1x90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x90 RCSB], [https://www.ebi.ac.uk/pdbsum/1x90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x90 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x90 OCA], [http://pdbe.org/1x90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x90 RCSB], [http://www.ebi.ac.uk/pdbsum/1x90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x90 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PMEI1_ARATH PMEI1_ARATH]] Inhibits pectin methylesterase from flowers and siliques.<ref>PMID:14675772</ref> | + | [https://www.uniprot.org/uniprot/PMEI1_ARATH PMEI1_ARATH] Inhibits pectin methylesterase from flowers and siliques.<ref>PMID:14675772</ref> |
| | == 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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aloy, P]] | + | [[Category: Aloy P]] |
| - | [[Category: Greiner, S]] | + | [[Category: Greiner S]] |
| - | [[Category: Hothorn, M]] | + | [[Category: Hothorn M]] |
| - | [[Category: Scheffzek, K]] | + | [[Category: Scheffzek K]] |
| - | [[Category: Wolf, S]] | + | [[Category: Wolf S]] |
| - | [[Category: Alpha hairpin]]
| + | |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Four-helix bundle]]
| + | |
| - | [[Category: Linker]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Proline]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
PMEI1_ARATH Inhibits pectin methylesterase from flowers and siliques.[1]
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 methylesterase (PME) and invertase are key enzymes in plant carbohydrate metabolism. Inhibitors of both enzymes constitute a sequence family of extracellular proteins. Members of this family are selectively targeted toward either PME or invertase. In a comparative structural approach we have studied how this target specificity is implemented on homologous sequences. By extending crystallographic work on the invertase inhibitor Nt-CIF to a pectin methylesterase inhibitor (PMEI) from Arabidopsis thaliana, we show an alpha-helical hairpin motif to be an independent and mobile structural entity in PMEI. Removal of this hairpin fully inactivates the inhibitor. A chimera composed of the alpha-hairpin of PMEI and the four-helix bundle of Nt-CIF is still active against PME. By contrast, combining the corresponding segment of Nt-CIF with the four-helix bundle of PMEI renders the protein inactive toward either PME or invertase. Our experiments provide insight in how these homologous inhibitors can make differential use of similar structural modules to achieve distinct functions. Integrating our results with previous findings, we present a model for the PME-PMEI complex with important implications.
Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins.,Hothorn M, Wolf S, Aloy P, Greiner S, Scheffzek K Plant Cell. 2004 Dec;16(12):3437-47. Epub 2004 Nov 4. PMID:15528298[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wolf S, Grsic-Rausch S, Rausch T, Greiner S. Identification of pollen-expressed pectin methylesterase inhibitors in Arabidopsis. FEBS Lett. 2003 Dec 18;555(3):551-5. PMID:14675772
- ↑ Hothorn M, Wolf S, Aloy P, Greiner S, Scheffzek K. Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins. Plant Cell. 2004 Dec;16(12):3437-47. Epub 2004 Nov 4. PMID:15528298 doi:10.1105/tpc.104.025684
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