2nsp

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[[Image:2nsp.jpg|left|200px]]
 
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==Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide I==
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The line below this paragraph, containing "STRUCTURE_2nsp", creates the "Structure Box" on the page.
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<StructureSection load='2nsp' size='340' side='right'caption='[[2nsp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2nsp]] 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=2NSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NSP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#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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{{STRUCTURE_2nsp| PDB=2nsp | SCENE= }}
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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=2nsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nsp OCA], [https://pdbe.org/2nsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nsp RCSB], [https://www.ebi.ac.uk/pdbsum/2nsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nsp 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/ns/2nsp_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=2nsp 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 D178A mutant in complex with hexasaccharide I'''
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2NSP is a [[Single protein]] structure of 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=2NSP OCA].
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</div>
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<div class="pdbe-citations 2nsp" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17717531 17717531]
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*[[Methylesterase 3D structures|Methylesterase 3D structures]]
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[[Category: Erwinia chrysanthemi]]
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== References ==
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[[Category: Pectinesterase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Brocklehurst, K.]]
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</StructureSection>
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[[Category: Fries, M.]]
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[[Category: Dickeya dadantii 3937]]
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[[Category: Pickersgill, R W.]]
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[[Category: Large Structures]]
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[[Category: Shevchik, V E.]]
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[[Category: Brocklehurst K]]
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[[Category: Hydrolase]]
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[[Category: Fries M]]
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[[Category: Michaelis complex]]
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[[Category: Pickersgill RW]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:51:54 2008''
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[[Category: Shevchik VE]]

Current revision

Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide I

PDB ID 2nsp

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