2ntq

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[[Image:2ntq.png|left|200px]]
 
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{{STRUCTURE_2ntq| PDB=2ntq | SCENE= }}
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==Crystal structure of pectin methylesterase in complex with hexasaccharide VII==
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<StructureSection load='2ntq' size='340' side='right'caption='[[2ntq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PMEA_DICD3 PMEA_DICD3] Involved in maceration and soft-rotting of plant tissue.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/2ntq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ntq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of pectin methylesterase in complex with hexasaccharide VII===
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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<ref>PMID:17717531</ref>
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{{ABSTRACT_PUBMED_17717531}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2ntq" style="background-color:#fffaf0;"></div>
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[[2ntq]] is a 2 chain structure of [[Methylesterase]] with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NTQ OCA].
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==See Also==
==See Also==
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*[[Methylesterase|Methylesterase]]
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*[[Methylesterase 3D structures|Methylesterase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017717531</ref><references group="xtra"/>
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__TOC__
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[[Category: Erwinia chrysanthemi]]
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</StructureSection>
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[[Category: Pectinesterase]]
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[[Category: Dickeya dadantii 3937]]
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[[Category: Brocklehurst, K.]]
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[[Category: Large Structures]]
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[[Category: Fries, M.]]
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[[Category: Brocklehurst K]]
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[[Category: Pickersgill, R W.]]
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[[Category: Fries M]]
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[[Category: Shevchik, V E.]]
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[[Category: Pickersgill RW]]
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[[Category: Hydrolase]]
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[[Category: Shevchik VE]]
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[[Category: Pme hexasaccharide complex]]
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Current revision

Crystal structure of pectin methylesterase in complex with hexasaccharide VII

PDB ID 2ntq

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