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| | <StructureSection load='2ntq' size='340' side='right'caption='[[2ntq]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2ntq' size='340' side='right'caption='[[2ntq]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ntq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dicd3 Dicd3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NTQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ntq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_dadantii_3937 Dickeya dadantii 3937]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NTQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=M8C:METHYL+ALPHA-D-GALACTOPYRANURONATE'>M8C</scene></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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qjv|1qjv]], [[2nsp|2nsp]], [[2nst|2nst]], [[2nt6|2nt6]], [[2nt9|2nt9]], [[2ntb|2ntb]], [[2ntp|2ntp]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <scene name='pdbligand=M8C:METHYL+ALPHA-D-GALACTOPYRANURONATE'>M8C</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pemA, pem ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198628 DICD3])</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>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ntq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ntq OCA], [https://pdbe.org/2ntq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ntq RCSB], [https://www.ebi.ac.uk/pdbsum/2ntq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ntq 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=2ntq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ntq OCA], [https://pdbe.org/2ntq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ntq RCSB], [https://www.ebi.ac.uk/pdbsum/2ntq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ntq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PMEA_DICD3 PMEA_DICD3]] Involved in maceration and soft-rotting of plant tissue.
| + | [https://www.uniprot.org/uniprot/PMEA_DICD3 PMEA_DICD3] Involved in maceration and soft-rotting of plant tissue. |
| | == 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: Dicd3]] | + | [[Category: Dickeya dadantii 3937]] |
| - | [[Category: Hydrolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brocklehurst, K]] | + | [[Category: Brocklehurst K]] |
| - | [[Category: Fries, M]] | + | [[Category: Fries M]] |
| - | [[Category: Pickersgill, R W]] | + | [[Category: Pickersgill RW]] |
| - | [[Category: Shevchik, V E]] | + | [[Category: Shevchik VE]] |
| - | [[Category: Pme hexasaccharide complex]]
| + | |
| Structural highlights
Function
PMEA_DICD3 Involved in maceration and soft-rotting of plant tissue.
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
We provide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the essential first step in bacterial invasion of plant tissues. The complexes formed in the crystal using specifically methylated pectins, together with kinetic measurements of directed mutants, provide clear insights at atomic resolution into the specificity and the processive action of the Erwinia chrysanthemi enzyme. Product complexes provide additional snapshots along the reaction coordinate. We previously revealed that PME is a novel aspartic-esterase possessing parallel beta-helix architecture and now show that the two conserved aspartates are the nucleophile and general acid-base in the mechanism, respectively. Other conserved residues at the catalytic centre are shown to be essential for substrate binding or transition state stabilisation. The preferential binding of methylated sugar residues upstream of the catalytic site, and demethylated residues downstream, drives the enzyme along the pectin molecule and accounts for the sequential pattern of demethylation produced by both bacterial and plant PMEs.
Molecular basis of the activity of the phytopathogen pectin methylesterase.,Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW EMBO J. 2007 Sep 5;26(17):3879-87. Epub 2007 Aug 23. PMID:17717531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW. Molecular basis of the activity of the phytopathogen pectin methylesterase. EMBO J. 2007 Sep 5;26(17):3879-87. Epub 2007 Aug 23. PMID:17717531
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