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1nkg

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(New page: 200px<br /><applet load="1nkg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nkg, resolution 1.50&Aring;" /> '''Rhamnogalacturonan l...)
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[[Image:1nkg.gif|left|200px]]<br /><applet load="1nkg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nkg, resolution 1.50&Aring;" />
 
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'''Rhamnogalacturonan lyase from Aspergillus aculeatus'''<br />
 
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==Overview==
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==Rhamnogalacturonan lyase from Aspergillus aculeatus==
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Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves, alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in, the backbone of rhamnogalacturonan-I, a major component of the plant cell, wall polysaccharide, pectin. The three-dimensional structure of RG-lyase, from Aspergillus aculeatus has been determined to 1.5 A resolution, representing the first known structure from polysaccharide lyase family 4, and of an enzyme with this catalytic specificity. The 508-amino acid, polypeptide displays a unique arrangement of three distinct modular, domains. Each domain shows structural homology to non-catalytic domains, from other carbohydrate active enzymes.
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<StructureSection load='1nkg' size='340' side='right'caption='[[1nkg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1nkg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NKG FirstGlance]. <br>
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1NKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NKG 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]] 1.5&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1nkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nkg OCA], [https://pdbe.org/1nkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nkg RCSB], [https://www.ebi.ac.uk/pdbsum/1nkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nkg ProSAT]</span></td></tr>
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Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4., McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S, FEBS Lett. 2004 May 7;565(1-3):188-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15135077 15135077]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RGLA_ASPAC RGLA_ASPAC] Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.<ref>PMID:20851126</ref> <ref>PMID:8587995</ref> <ref>PMID:9576783</ref>
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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/nk/1nkg_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=1nkg ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Aspergillus aculeatus]]
[[Category: Aspergillus aculeatus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Harris, P.]]
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[[Category: Harris P]]
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[[Category: Kadirvelraj, R.]]
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[[Category: Kadirvelraj R]]
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[[Category: Larsen, S.]]
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[[Category: Larsen S]]
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[[Category: McDonough, M.A.]]
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[[Category: McDonough MA]]
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[[Category: Poulsen, J.C.]]
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[[Category: Poulsen JC]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: carbohydrate active enzyme]]
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[[Category: pectin]]
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[[Category: polysaccharide lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:19:59 2007''
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Current revision

Rhamnogalacturonan lyase from Aspergillus aculeatus

PDB ID 1nkg

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