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1idk

From Proteopedia

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[[Image:1idk.gif|left|200px]]<br />
 
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<applet load="1idk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1idk, resolution 1.93&Aring;" />
 
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'''PECTIN LYASE A'''<br />
 
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==Overview==
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==PECTIN LYASE A==
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BACKGROUND: Microbial pectin and pectate lyases are virulence factors that, degrade the pectic components of the plant cell wall. The homogalacturan, backbone of pectin varies in its degree of methylation from the highly, methylated and relatively hydrophobic form known as pectin, to the fully, demethylated and highly charged form known as pectate. Methylated and, demethylated regions of pectin are cleaved by pectin lyase and, calcium-dependent pectate lyases, respectively. Protein engineering of, lyases specific for particular patterns of methylation, will yield, modified pectins of high value to the food and pharmaceutical industries., RESULTS: The crystal structures of pectin lyase A from two strains of, Aspergillus niger, N400 and 4M-147, have been determined at pH 6.5 (2.4 A, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9195887 (full description)]]
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<StructureSection load='1idk' size='340' side='right'caption='[[1idk]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1idk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDK FirstGlance]. <br>
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1IDK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]]. Active as [[http://en.wikipedia.org/wiki/Pectin_lyase Pectin lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.10 4.2.2.10]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDK OCA]].
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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]] 1.93&#8491;</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=1idk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idk OCA], [https://pdbe.org/1idk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idk RCSB], [https://www.ebi.ac.uk/pdbsum/1idk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idk ProSAT]</span></td></tr>
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==Reference==
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</table>
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Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases., Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J, Structure. 1997 May 15;5(5):677-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9195887 9195887]
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== Function ==
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[https://www.uniprot.org/uniprot/PELA_ASPNG PELA_ASPNG] Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
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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/id/1idk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1idk ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
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[[Category: Pectin lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Benen J]]
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[[Category: Benen, J.]]
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[[Category: Connerton I]]
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[[Category: Connerton, I.]]
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[[Category: Gravesen T]]
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[[Category: Gravesen, T.]]
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[[Category: Jenkins J]]
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[[Category: Jenkins, J.]]
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[[Category: Mayans O]]
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[[Category: Mayans, O.]]
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[[Category: Pickersgill R]]
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[[Category: Pickersgill, R.]]
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[[Category: Scott M]]
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[[Category: Scott, M.]]
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[[Category: Visser J]]
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[[Category: Visser, J.]]
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[[Category: glycoprotein]]
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[[Category: lyase]]
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[[Category: multigene family]]
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[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:39:13 2007''
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Current revision

PECTIN LYASE A

PDB ID 1idk

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